1btj - Revision history

OCA at 15:35, 13 March 2024

OCA — Wed, 13 Mar 2024 15:35:57 GMT

←Older revision		Revision as of 15:35, 13 March 2024
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	<StructureSection load='1btj' size='340' side='right'caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='1btj' size='340' side='right'caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>
-	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [https://pdbe.org/1btj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [https://www.ebi.ac.uk/pdbsum/1btj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btj ProSAT]</span></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]] 3.2Å</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [https://pdbe.org/1btj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [https://www.ebi.ac.uk/pdbsum/1btj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[https://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>	+	[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[https://omim.org/entry/209300 209300]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.	+	[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 21:
	</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=1btj 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=1btj ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Serum transferrin binds ferric ions in the bloodstream and transports them to cells, where they are released in a process involving receptor-mediated endocytosis. Iron release is believed to be pH dependent and is coupled with a large conformational change. To help define the steps in iron release, we have determined the three-dimensional structure of the iron-free (apo) form of the recombinant N-lobe half-molecule of human serum transferrin (ApoTfN) by X-ray crystallography. Two crystal forms were obtained, form 1 with four molecules in the asymmetric unit and form 2 with two molecules in the asymmetric unit. The structures of both forms were determined by molecular replacement and were refined at 2.2 and 3.2 A resolution, respectively. Final R-factors were 0.203 (free R = 0. 292) for form 1 and 0.217 (free R = 0.312) for form 2. All six copies of the ApoTfN structure are essentially identical. Comparison with the holo form (FeTfN) shows that a large rigid-body domain movement of 63 degrees has occurred in ApoTfN, to give an open binding cleft. The extent of domain opening is the same as in the N-lobe of human lactoferrin, showing that it depends on internal constraints that are conserved in both proteins, and that it is unaffected by the presence or absence of the C-lobe. Although the conformational change is primarily a rigid-body motion, several local adjustments occur. In particular, two iron ligands, Asp 63 and His 249, change conformation to form salt bridges, with Lys 296 and Glu 83, respectively, in the binding cleft of the apo protein. Both salt bridges would have to break for iron coordination to occur. Most importantly, the structure, determined at a pH (5.3) that is close to the pH of physiological iron release, indicates that protonation of His 249 is a key step in iron release.
-
-	Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin.,Jeffrey PD, Bewley MC, MacGillivray RT, Mason AB, Woodworth RC, Baker EN Biochemistry. 1998 Oct 6;37(40):13978-86. PMID:9760232<ref>PMID:9760232</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1btj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Baker~~, E N~~]]	+	[[Category: Baker EN]]
-	[[Category: Bewley~~, M C~~]]	+	[[Category: Bewley MC]]
-	[[Category: Jeffrey~~, P D~~]]	+	[[Category: Jeffrey PD]]
-	[[Category: Macgillivray~~, R T.A~~]]	+	[[Category: Macgillivray RTA]]
-	[[Category: Mason~~, A B~~]]	+	[[Category: Mason AB]]
-	[[Category: Woodworth~~, R C]]~~	+	[[Category: Woodworth RC]]
-	~~[[Category: Conformational change]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Iron transport]]~~	+
-	~~[[Category: Iron-free form]]~~	+
-	~~[[Category: Metal transport]]~~	+
-	~~[[Category: N-lobe]]~~	+
-	~~[[Category: Transferrin~~]]	+

OCA at 09:49, 15 September 2021

OCA — Wed, 15 Sep 2021 09:49:27 GMT

←Older revision		Revision as of 09:49, 15 September 2021
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	<StructureSection load='1btj' size='340' side='right'caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='1btj' size='340' side='right'caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>
-	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [~~http~~://pdbe.org/1btj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1btj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1btj ProSAT]</span></td></tr>	+	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [https://pdbe.org/1btj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [https://www.ebi.ac.uk/pdbsum/1btj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[~~http~~://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>	+	[[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[https://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.	+	[[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Transferrin\|Transferrin]]	+	*[[Transferrin 3D structures\|Transferrin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:45, 14 August 2019

OCA — Wed, 14 Aug 2019 17:45:01 GMT

←Older revision		Revision as of 17:45, 14 August 2019
Line 1:		Line 1:

	==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2==		==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2==
-	<StructureSection load='1btj' size='340' side='right' caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>	+	<StructureSection load='1btj' size='340' side='right'caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bt/1btj_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bt/1btj_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 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1btj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1btj" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]
	[[Category: Bewley, M C]]		[[Category: Bewley, M C]]

OCA at 10:45, 8 November 2017

OCA — Wed, 08 Nov 2017 10:45:24 GMT

←Older revision		Revision as of 10:45, 8 November 2017
Line 1:		Line 1:
		+
	==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2==		==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2==
	<StructureSection load='1btj' size='340' side='right' caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='1btj' size='340' side='right' caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>
-	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [http://pdbe.org/1btj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [http://www.ebi.ac.uk/pdbsum/1btj PDBsum]</span></td></tr>	+	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [http://pdbe.org/1btj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [http://www.ebi.ac.uk/pdbsum/1btj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1btj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1btj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1btj" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:19, 7 February 2016

OCA — Sun, 07 Feb 2016 14:19:32 GMT

←Older revision		Revision as of 14:19, 7 February 2016
Line 17:		Line 17:
	<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=1btj ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:19, 10 September 2015

OCA — Thu, 10 Sep 2015 02:19:08 GMT

←Older revision		Revision as of 02:19, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1btj' size='340' side='right' caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='1btj' size='340' side='right' caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>
-	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [http://www.ebi.ac.uk/pdbsum/1btj PDBsum]</span></td></tr>	+	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [http://pdbe.org/1btj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [http://www.ebi.ac.uk/pdbsum/1btj PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 27:		Line 27:
	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 1btj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]
	[[Category: Bewley, M C]]		[[Category: Bewley, M C]]

OCA at 10:34, 22 December 2014

OCA — Mon, 22 Dec 2014 10:34:41 GMT

←Older revision		Revision as of 10:34, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>
-	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [http://www.ebi.ac.uk/pdbsum/1btj PDBsum]</span></td></tr>	+	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [http://www.ebi.ac.uk/pdbsum/1btj PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>		[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Baker, E N.]]	+	[[Category: Baker, E N]]
-	[[Category: Bewley, M C.]]	+	[[Category: Bewley, M C]]
-	[[Category: Jeffrey, P D.]]	+	[[Category: Jeffrey, P D]]
-	[[Category: Macgillivray, R T.A.]]	+	[[Category: Macgillivray, R T.A]]
-	[[Category: Mason, A B.]]	+	[[Category: Mason, A B]]
-	[[Category: Woodworth, R C.]]	+	[[Category: Woodworth, R C]]
	[[Category: Conformational change]]		[[Category: Conformational change]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]

OCA at 16:49, 29 September 2014

OCA — Mon, 29 Sep 2014 16:49:27 GMT

←Older revision		Revision as of 16:49, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1btj\| PDB=1btj \| SCENE= }}~~	+	==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2==
-	===HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2===	+	<StructureSection load='1btj' size='340' side='right' caption='[[1btj]], [[Resolution\|resolution]] 3.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_9760232}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1btj]] is a 2 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=1BTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTJ FirstGlance]. <br>
		+	</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=1btj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1btj RCSB], [http://www.ebi.ac.uk/pdbsum/1btj PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
		+	== 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/bt/1btj_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 ==
		+	Serum transferrin binds ferric ions in the bloodstream and transports them to cells, where they are released in a process involving receptor-mediated endocytosis. Iron release is believed to be pH dependent and is coupled with a large conformational change. To help define the steps in iron release, we have determined the three-dimensional structure of the iron-free (apo) form of the recombinant N-lobe half-molecule of human serum transferrin (ApoTfN) by X-ray crystallography. Two crystal forms were obtained, form 1 with four molecules in the asymmetric unit and form 2 with two molecules in the asymmetric unit. The structures of both forms were determined by molecular replacement and were refined at 2.2 and 3.2 A resolution, respectively. Final R-factors were 0.203 (free R = 0. 292) for form 1 and 0.217 (free R = 0.312) for form 2. All six copies of the ApoTfN structure are essentially identical. Comparison with the holo form (FeTfN) shows that a large rigid-body domain movement of 63 degrees has occurred in ApoTfN, to give an open binding cleft. The extent of domain opening is the same as in the N-lobe of human lactoferrin, showing that it depends on internal constraints that are conserved in both proteins, and that it is unaffected by the presence or absence of the C-lobe. Although the conformational change is primarily a rigid-body motion, several local adjustments occur. In particular, two iron ligands, Asp 63 and His 249, change conformation to form salt bridges, with Lys 296 and Glu 83, respectively, in the binding cleft of the apo protein. Both salt bridges would have to break for iron coordination to occur. Most importantly, the structure, determined at a pH (5.3) that is close to the pH of physiological iron release, indicates that protonation of His 249 is a key step in iron release.

-	~~==Disease==~~	+	Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin.,Jeffrey PD, Bewley MC, MacGillivray RT, Mason AB, Woodworth RC, Baker EN Biochemistry. 1998 Oct 6;37(40):13978-86. PMID:9760232<ref>PMID:9760232</ref>
-	~~[[http~~:~~//www~~.~~uniprot~~.~~org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia~~ (~~ATRAF~~) ~~[MIM~~:~~[http://omim~~.~~org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>~~PMID:~~11110675</ref>~~<ref>PMID:~~15466165~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding~~ of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1btj]] is a 2 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=1BTJ OCA].~~	+

	==See Also==		==See Also==
	*[[Transferrin\|Transferrin]]		*[[Transferrin\|Transferrin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:009760232</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Baker, E N.]]		[[Category: Baker, E N.]]

OCA at 20:34, 24 March 2013

OCA — Sun, 24 Mar 2013 20:34:24 GMT

←Older revision		Revision as of 20:34, 24 March 2013
Line 1:		Line 1:
-	[[Image:1btj.png\|left\|200px]]
-
	{{STRUCTURE_1btj\| PDB=1btj \| SCENE= }}		{{STRUCTURE_1btj\| PDB=1btj \| SCENE= }}
-
	===HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2===		===HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2===
		+	{{ABSTRACT_PUBMED_9760232}}

-	~~{{ABSTRACT_PUBMED_9760232}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref><ref>PMID:15466165</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:009760232</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009760232</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Baker, E N.]]		[[Category: Baker, E N.]]

OCA at 06:54, 20 October 2012

OCA — Sat, 20 Oct 2012 06:54:10 GMT

←Older revision		Revision as of 06:54, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1btj]] is a 2 chain structure ~~of [[Transferrin]]~~ 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=1BTJ OCA].	+	[[1btj]] is a 2 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=1BTJ OCA].

	==See Also==		==See Also==