1xmi - Revision history

OCA at 06:47, 23 August 2023

OCA — Wed, 23 Aug 2023 06:47:44 GMT

←Older revision		Revision as of 06:47, 23 August 2023
Line 3:		Line 3:
	<StructureSection load='1xmi' size='340' side='right'caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1xmi' size='340' side='right'caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XMI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XMI FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ATP:ADENOSINE~~-~~5-TRIPHOSPHATE'>ATP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.25Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>CFTR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>[https://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [https://pdbe.org/1xmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [https://www.ebi.ac.uk/pdbsum/1xmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmi ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [https://pdbe.org/1xmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [https://www.ebi.ac.uk/pdbsum/1xmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmi ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[https://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[https://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]	+	[https://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[https://omim.org/entry/219700 219700]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[https://omim.org/entry/277180 277180]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>	+	[https://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Channel-conductance-controlling ATPase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Condon, B]]	+	[[Category: Condon B]]
-	[[Category: Conners, K]]	+	[[Category: Conners K]]
-	[[Category: Emtage, S]]	+	[[Category: Emtage S]]
-	~~[[Category: GenomiX, Structural~~]]	+	[[Category: Guggino WB]]
-	[[Category: Guggino~~, W B~~]]	+	[[Category: Hunt JF]]
-	[[Category: Hunt~~, J F~~]]	+	[[Category: Kearins MC]]
-	[[Category: Kearins~~, M C~~]]	+	[[Category: Lewis HA]]
-	[[Category: Lewis~~, H A~~]]	+	[[Category: Lorimer D]]
-	[[Category: Lorimer, D]]	+	[[Category: Maloney PC]]
-	[[Category: Maloney~~, P C~~]]	+	[[Category: Noland BW]]
-	[[Category: Noland~~, B W~~]]	+	[[Category: Rooney I]]
-	[[Category: Rooney, I]]	+	[[Category: Sauder JM]]
-	[[Category: Sauder~~, J M~~]]	+	[[Category: Structural GenomiX]]
-	[[Category: ~~Wang, C~~]]	+	[[Category: Wang C]]
-	[[Category: ~~Zhao, X~~]]	+	[[Category: Zhao X]]
-	[[Category: ~~Cftr]]~~	+
-	~~[[Category: Cystic fibrosis]]~~	+
-	~~[[Category: F508a]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Nbd1 domain]]~~	+
-	~~[[Category: Nucleotide-binding domain 1~~]]	+

OCA at 16:42, 20 October 2021

OCA — Wed, 20 Oct 2021 16:42:38 GMT

OCA at 10:07, 6 January 2021

OCA — Wed, 06 Jan 2021 10:07:43 GMT

←Older revision		Revision as of 10:07, 6 January 2021
Line 1:		Line 1:

	==Crystal structure of human F508A NBD1 domain with ATP==		==Crystal structure of human F508A NBD1 domain with ATP==
-	<StructureSection load='1xmi' size='340' side='right' caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>	+	<StructureSection load='1xmi' size='340' side='right'caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1XMI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XMI FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://pdbe.org/1xmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmi ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://pdbe.org/1xmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmi ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 35:		Line 35:

	==See Also==		==See Also==
-	*[[ABC transporter\|ABC transporter]]	+	*[[ABC transporter 3D structures\|ABC transporter 3D structures]]
-	*[[Ion channels\|Ion channels]]	+
	== References ==		== References ==
	<references/>		<references/>
Line 43:		Line 42:
	[[Category: Channel-conductance-controlling ATPase]]		[[Category: Channel-conductance-controlling ATPase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Condon, B]]		[[Category: Condon, B]]
	[[Category: Conners, K]]		[[Category: Conners, K]]

OCA at 08:25, 14 November 2018

OCA — Wed, 14 Nov 2018 08:25:12 GMT

←Older revision		Revision as of 08:25, 14 November 2018
Line 18:		Line 18:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xmi_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xmi_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:
	</div>		</div>
	<div class="pdbe-citations 1xmi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1xmi" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ABC transporter\|ABC transporter]]
		+	*[[Ion channels\|Ion channels]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:22, 12 October 2017

OCA — Thu, 12 Oct 2017 10:22:35 GMT

←Older revision		Revision as of 10:22, 12 October 2017
Line 1:		Line 1:
		+
	==Crystal structure of human F508A NBD1 domain with ATP==		==Crystal structure of human F508A NBD1 domain with ATP==
	<StructureSection load='1xmi' size='340' side='right' caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1xmi' size='340' side='right' caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://pdbe.org/1xmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://pdbe.org/1xmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmi ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 32:		Line 33:
	</div>		</div>
	<div class="pdbe-citations 1xmi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1xmi" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[ABC transporter\|ABC transporter]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:11, 7 February 2016

OCA — Sun, 07 Feb 2016 20:11:49 GMT

←Older revision		Revision as of 20:11, 7 February 2016
Line 21:		Line 21:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xmi ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:37, 10 September 2015

OCA — Thu, 10 Sep 2015 04:37:47 GMT

←Older revision		Revision as of 04:37, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1xmi' size='340' side='right' caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1xmi' size='340' side='right' caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XMI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XMI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://pdbe.org/1xmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 31:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1xmi" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Channel-conductance-controlling ATPase]]		[[Category: Channel-conductance-controlling ATPase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Condon, B]]		[[Category: Condon, B]]
	[[Category: Conners, K]]		[[Category: Conners, K]]

OCA at 13:21, 6 January 2015

OCA — Tue, 06 Jan 2015 13:21:45 GMT

←Older revision		Revision as of 13:21, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XMI FirstGlance]. <br>		<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XMI FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[http://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[http://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]		[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[http://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[http://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]
Line 40:		Line 40:
	[[Category: Channel-conductance-controlling ATPase]]		[[Category: Channel-conductance-controlling ATPase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Condon, B.]]	+	[[Category: Condon, B]]
-	[[Category: Conners, K.]]	+	[[Category: Conners, K]]
-	[[Category: Emtage, S.]]	+	[[Category: Emtage, S]]
-	[[Category: GenomiX, Structural.]]	+	[[Category: GenomiX, Structural]]
-	[[Category: Guggino, W B.]]	+	[[Category: Guggino, W B]]
-	[[Category: Hunt, J F.]]	+	[[Category: Hunt, J F]]
-	[[Category: Kearins, M C.]]	+	[[Category: Kearins, M C]]
-	[[Category: Lewis, H A.]]	+	[[Category: Lewis, H A]]
-	[[Category: Lorimer, D.]]	+	[[Category: Lorimer, D]]
-	[[Category: Maloney, P C.]]	+	[[Category: Maloney, P C]]
-	[[Category: Noland, B W.]]	+	[[Category: Noland, B W]]
-	[[Category: Rooney, I.]]	+	[[Category: Rooney, I]]
-	[[Category: Sauder, J M.]]	+	[[Category: Sauder, J M]]
-	[[Category: Wang, C.]]	+	[[Category: Wang, C]]
-	[[Category: Zhao, X.]]	+	[[Category: Zhao, X]]
	[[Category: Cftr]]		[[Category: Cftr]]
	[[Category: Cystic fibrosis]]		[[Category: Cystic fibrosis]]

OCA at 18:52, 29 September 2014

OCA — Mon, 29 Sep 2014 18:52:43 GMT

←Older revision		Revision as of 18:52, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1xmi~~\| ~~PDB~~=1xmi \| ~~SCENE~~= }}	+	==Crystal structure of human F508A NBD1 domain with ATP==
-	===~~Crystal~~ structure of ~~human F508A NBD1 domain with ATP~~===	+	<StructureSection load='1xmi' size='340' side='right' caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>
-	~~{{ABSTRACT_PUBMED_15528182}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XMI FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [http://www.ebi.ac.uk/pdbsum/1xmi PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[http://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[http://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xmi_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cystic fibrosis is caused by defects in the cystic fibrosis transmembrane conductance regulator (CFTR), commonly the deletion of residue Phe-508 (DeltaF508) in the first nucleotide-binding domain (NBD1), which results in a severe reduction in the population of functional channels at the epithelial cell surface. Previous studies employing incomplete NBD1 domains have attributed this to aberrant folding of DeltaF508 NBD1. We report structural and biophysical studies on complete human NBD1 domains, which fail to demonstrate significant changes of in vitro stability or folding kinetics in the presence or absence of the DeltaF508 mutation. Crystal structures show minimal changes in protein conformation but substantial changes in local surface topography at the site of the mutation, which is located in the region of NBD1 believed to interact with the first membrane spanning domain of CFTR. These results raise the possibility that the primary effect of DeltaF508 is a disruption of proper interdomain interactions at this site in CFTR rather than interference with the folding of NBD1. Interestingly, increases in the stability of NBD1 constructs are observed upon introduction of second-site mutations that suppress the trafficking defect caused by the DeltaF508 mutation, suggesting that these suppressors might function indirectly by improving the folding efficiency of NBD1 in the context of the full-length protein. The human NBD1 structures also solidify the understanding of CFTR regulation by showing that its two protein segments that can be phosphorylated both adopt multiple conformations that modulate access to the ATPase active site and functional interdomain interfaces.

-	~~==Disease==~~	+	Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure.,Lewis HA, Zhao X, Wang C, Sauder JM, Rooney I, Noland BW, Lorimer D, Kearins MC, Conners K, Condon B, Maloney PC, Guggino WB, Hunt JF, Emtage S J Biol Chem. 2005 Jan 14;280(2):1346-53. Epub 2004 Nov 3. PMID:15528182<ref>PMID:15528182</ref>
-	~~[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects~~ in ~~CFTR are the cause~~ of cystic fibrosis ~~(CF) [MIM:[http://omim~~.~~org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population~~, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), ~~pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes~~.<ref>PMID:1695717</ref><ref>PMID:2236053</ref><ref>PMID:1710600</ref><ref>PMID:1284466</ref><ref>PMID:1284468</ref><ref>PMID:1284530</ref><ref>PMID:1284529</ref><ref>PMID:7680525</ref><ref>PMID:7683628</ref><ref>PMID:7683954</ref><ref>PMID:7505694</ref><ref>PMID:7504969</ref><ref>PMID:7522211</ref><ref>PMID:7513296</ref><ref>PMID:7525450</ref><ref>PMID:7520022</ref><ref>PMID:7524913</ref><ref>PMID:7524909</ref><ref>PMID:7517264</ref><ref>PMID:8081395</ref><ref>PMID:7544319</ref><ref>PMID:8522333</ref><ref>PMID:7537150</ref><ref>PMID:7541273</ref><ref>PMID:7581407</ref><ref>PMID:7543567</ref><ref>PMID:7541510</ref><ref>PMID:8800923</ref><ref>PMID:8829633</ref><ref>PMID:8723693</ref><ref>PMID:8723695</ref><ref>PMID:8956039</ref><ref>PMID:9101301</ref><ref>PMID:9222768</ref><ref>PMID:9375855</ref><ref>PMID:9401006</ref><ref>PMID:9443874</ref><ref>PMID:9521595</ref><ref>PMID:9921909</ref><ref>PMID:9736778</ref><ref>PMID:9482579</ref><ref>PMID:9554753</ref><ref>PMID:9452048</ref><ref>PMID:9452054</ref><ref>PMID:9452073</ref><ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (~~CBAVD~~) ~~[MIM~~:~~[http://omim~~.~~org/entry/277180 277180]]~~. ~~CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>~~PMID:~~7529962</ref>~~<ref>PMID:~~7539342~~</ref>~~<ref>PMID:9067761</ref><ref>PMID:10651488</ref>[:]~~	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport~~ of ~~chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating~~ the ~~SLC4A7 transporter~~. ~~Can inhibit the chloride channel activity~~ of ~~ANO1~~.<~~ref~~>~~PMID:22178883~~</~~ref~~>	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[1xmi]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA].	+

	==See Also==		==See Also==
	*[[ABC transporter\|ABC transporter]]		*[[ABC transporter\|ABC transporter]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:015528182</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Channel-conductance-controlling ATPase]]		[[Category: Channel-conductance-controlling ATPase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 23:51, 24 March 2013

OCA — Sun, 24 Mar 2013 23:51:35 GMT

←Older revision		Revision as of 23:51, 24 March 2013
Line 1:		Line 1:
-	[[Image:1xmi.png\|left\|200px]]
-
	{{STRUCTURE_1xmi\| PDB=1xmi \| SCENE= }}		{{STRUCTURE_1xmi\| PDB=1xmi \| SCENE= }}
-
	===Crystal structure of human F508A NBD1 domain with ATP===		===Crystal structure of human F508A NBD1 domain with ATP===
		+	{{ABSTRACT_PUBMED_15528182}}

-	~~{{ABSTRACT_PUBMED_15528182}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[http://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref><ref>PMID:2236053</ref><ref>PMID:1710600</ref><ref>PMID:1284466</ref><ref>PMID:1284468</ref><ref>PMID:1284530</ref><ref>PMID:1284529</ref><ref>PMID:7680525</ref><ref>PMID:7683628</ref><ref>PMID:7683954</ref><ref>PMID:7505694</ref><ref>PMID:7504969</ref><ref>PMID:7522211</ref><ref>PMID:7513296</ref><ref>PMID:7525450</ref><ref>PMID:7520022</ref><ref>PMID:7524913</ref><ref>PMID:7524909</ref><ref>PMID:7517264</ref><ref>PMID:8081395</ref><ref>PMID:7544319</ref><ref>PMID:8522333</ref><ref>PMID:7537150</ref><ref>PMID:7541273</ref><ref>PMID:7581407</ref><ref>PMID:7543567</ref><ref>PMID:7541510</ref><ref>PMID:8800923</ref><ref>PMID:8829633</ref><ref>PMID:8723693</ref><ref>PMID:8723695</ref><ref>PMID:8956039</ref><ref>PMID:9101301</ref><ref>PMID:9222768</ref><ref>PMID:9375855</ref><ref>PMID:9401006</ref><ref>PMID:9443874</ref><ref>PMID:9521595</ref><ref>PMID:9921909</ref><ref>PMID:9736778</ref><ref>PMID:9482579</ref><ref>PMID:9554753</ref><ref>PMID:9452048</ref><ref>PMID:9452054</ref><ref>PMID:9452073</ref><ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[http://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref><ref>PMID:7539342</ref><ref>PMID:9067761</ref><ref>PMID:10651488</ref>[:]
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:015528182</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015528182</ref><references group="xtra"/><references/>
	[[Category: Channel-conductance-controlling ATPase]]		[[Category: Channel-conductance-controlling ATPase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

←Older revision		Revision as of 16:42, 20 October 2021
Line 3:		Line 3:
	<StructureSection load='1xmi' size='340' side='right'caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1xmi' size='340' side='right'caption='[[1xmi]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1XMI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1xmi]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XMI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xmj\|1xmj]], [[1q3h\|1q3h]], [[1r0w\|1r0w]], [[1r0x\|1r0x]], [[1r0y\|1r0y]], [[1r0z\|1r0z]], [[1r10\|1r10]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CFTR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Channel-conductance-controlling_ATPase Channel-conductance-controlling ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.49 3.6.3.49] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [~~http~~://pdbe.org/1xmi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1xmi PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmi ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmi OCA], [https://pdbe.org/1xmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xmi RCSB], [https://www.ebi.ac.uk/pdbsum/1xmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmi ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[~~http~~://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[~~http~~://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]	+	[[https://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Defects in CFTR are the cause of cystic fibrosis (CF) [MIM:[https://omim.org/entry/219700 219700]]; also known as mucoviscidosis. CF is the most common genetic disease in the Caucasian population, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. CF is a common generalized disorder of exocrine gland function which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes.<ref>PMID:1695717</ref> <ref>PMID:2236053</ref> <ref>PMID:1710600</ref> <ref>PMID:1284466</ref> <ref>PMID:1284468</ref> <ref>PMID:1284530</ref> <ref>PMID:1284529</ref> <ref>PMID:7680525</ref> <ref>PMID:7683628</ref> <ref>PMID:7683954</ref> <ref>PMID:7505694</ref> <ref>PMID:7504969</ref> <ref>PMID:7522211</ref> <ref>PMID:7513296</ref> <ref>PMID:7525450</ref> <ref>PMID:7520022</ref> <ref>PMID:7524913</ref> <ref>PMID:7524909</ref> <ref>PMID:7517264</ref> <ref>PMID:8081395</ref> <ref>PMID:7544319</ref> <ref>PMID:8522333</ref> <ref>PMID:7537150</ref> <ref>PMID:7541273</ref> <ref>PMID:7581407</ref> <ref>PMID:7543567</ref> <ref>PMID:7541510</ref> <ref>PMID:8800923</ref> <ref>PMID:8829633</ref> <ref>PMID:8723693</ref> <ref>PMID:8723695</ref> <ref>PMID:8956039</ref> <ref>PMID:9101301</ref> <ref>PMID:9222768</ref> <ref>PMID:9375855</ref> <ref>PMID:9401006</ref> <ref>PMID:9443874</ref> <ref>PMID:9521595</ref> <ref>PMID:9921909</ref> <ref>PMID:9736778</ref> <ref>PMID:9482579</ref> <ref>PMID:9554753</ref> <ref>PMID:9452048</ref> <ref>PMID:9452054</ref> <ref>PMID:9452073</ref> <ref>PMID:10094564</ref> Defects in CFTR are the cause of congenital bilateral absence of the vas deferens (CBAVD) [MIM:[https://omim.org/entry/277180 277180]]. CBAVD is an important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.<ref>PMID:7529962</ref> <ref>PMID:7539342</ref> <ref>PMID:9067761</ref> <ref>PMID:10651488</ref> [:]
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>	+	[[https://www.uniprot.org/uniprot/CFTR_HUMAN CFTR_HUMAN]] Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1.<ref>PMID:22178883</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]