1a8e - Revision history

OCA at 15:22, 13 March 2024

OCA — Wed, 13 Mar 2024 15:22:05 GMT

←Older revision		Revision as of 15:22, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='1a8e' size='340' side='right'caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='1a8e' size='340' side='right'caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.6Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [https://pdbe.org/1a8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [https://www.ebi.ac.uk/pdbsum/1a8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8e 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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [https://pdbe.org/1a8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [https://www.ebi.ac.uk/pdbsum/1a8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8e 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 21:		Line 22:
	</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=1a8e 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=1a8e ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The N-lobe of human serum transferrin (hTF/2N) has been expressed in baby hamster kidney cells and crystallized in both orthorhombic (P212121) and tetragonal (P41212) space groups. Both crystal forms diffract to high resolution (1.6 and 1.8 A, respectively) and have been solved by molecular replacement. Subsequent refinement resulted in final models for the structure of hTF/2N that had crystallographic R-factors of 18.1 and 19.7% for the two crystal forms, respectively; these models represent the highest-resolution transferrin structures determined to date. The hTF/2N polypeptide has a folding pattern similar to those of other transferrins, including the presence of a deep cleft that contains the metal-binding site. In contrast to other transferrins, both crystal forms of hTF/2N display disorder at the iron-binding site; model building suggests that this disorder consists of alternative conformations of the synergistically bound carbonate anion, the side chain for Arg-124, and several solvent molecules. Subsequent refinement revealed that conformation A has an occupancy of 0.63-0. 65 and corresponds to the structure of the iron-binding site found in other transferrins. The alternative conformation B has an occupancy of 0.35-0.37; in this structure, the carbonate has rotated 30 degrees relative to the iron and the side chain for Arg-124 has moved to accommodate the new carbonate position. Several water molecules appear to stabilize the carbonate anion in the two conformations. These structures are consistent with the protonation of the carbonate and resulting partial removal of the anion from the metal; these events would occur prior to cleft opening and metal release.
-
-	Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release.,MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN Biochemistry. 1998 Jun 2;37(22):7919-28. PMID:9609685<ref>PMID:9609685</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1a8e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Anderson~~, B F~~]]	+	[[Category: Anderson BF]]
-	[[Category: Baker~~, E N~~]]	+	[[Category: Baker EN]]
-	[[Category: Baker, H]]	+	[[Category: Baker H]]
-	[[Category: Bewley, M]]	+	[[Category: Bewley M]]
-	[[Category: Brayer~~, G D~~]]	+	[[Category: Brayer GD]]
-	[[Category: Chen, J]]	+	[[Category: Chen J]]
-	[[Category: Luo, Y]]	+	[[Category: Luo Y]]
-	[[Category: Macgillivray~~, R T.A~~]]	+	[[Category: Macgillivray RTA]]
-	[[Category: Mason~~, A B~~]]	+	[[Category: Mason AB]]
-	[[Category: Moore~~, S A~~]]	+	[[Category: Moore SA]]
-	[[Category: Murphy~~, M E.P~~]]	+	[[Category: Murphy MEP]]
-	[[Category: Smith~~, C A~~]]	+	[[Category: Smith CA]]
-	[[Category: Wang, Y]]	+	[[Category: Wang Y]]
-	[[Category: Woodworth~~, R C]]~~	+	[[Category: Woodworth RC]]
-	~~[[Category: Carbonate]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Iron transport]]~~	+
-	~~[[Category: Iron-release]]~~	+
-	~~[[Category: Nlobe]]~~	+
-	~~[[Category: Transferrin~~]]	+

OCA at 09:43, 26 May 2021

OCA — Wed, 26 May 2021 09:43:32 GMT

←Older revision		Revision as of 09:43, 26 May 2021
Line 3:		Line 3:
	<StructureSection load='1a8e' size='340' side='right'caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='1a8e' size='340' side='right'caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1A8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [~~http~~://pdbe.org/1a8e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1a8e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8e 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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [https://pdbe.org/1a8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [https://www.ebi.ac.uk/pdbsum/1a8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8e 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 32:		Line 32:

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

OCA at 07:15, 21 August 2019

OCA — Wed, 21 Aug 2019 07:15:19 GMT

←Older revision		Revision as of 07:15, 21 August 2019
Line 1:		Line 1:

	==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE==		==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE==
-	<StructureSection load='1a8e' size='340' side='right' caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>	+	<StructureSection load='1a8e' size='340' side='right'caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8e_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8e_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 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1a8e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1a8e" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Anderson, B F]]		[[Category: Anderson, B F]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]

OCA at 10:42, 15 November 2017

OCA — Wed, 15 Nov 2017 10:42:53 GMT

←Older revision		Revision as of 10:42, 15 November 2017
Line 1:		Line 1:
		+
	==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE==		==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE==
	<StructureSection load='1a8e' size='340' side='right' caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='1a8e' size='340' side='right' caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [http://pdbe.org/1a8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [http://www.ebi.ac.uk/pdbsum/1a8e 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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [http://pdbe.org/1a8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [http://www.ebi.ac.uk/pdbsum/1a8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8e ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1a8e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1a8e" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:06, 8 February 2016

OCA — Mon, 08 Feb 2016 11:06:48 GMT

←Older revision		Revision as of 11:06, 8 February 2016
Line 18:		Line 18:
	<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=1a8e ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:56, 9 September 2015

OCA — Wed, 09 Sep 2015 15:56:10 GMT

←Older revision		Revision as of 15:56, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1a8e' size='340' side='right' caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='1a8e' size='340' side='right' caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [http://www.ebi.ac.uk/pdbsum/1a8e 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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [http://pdbe.org/1a8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [http://www.ebi.ac.uk/pdbsum/1a8e PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		Line 28:
	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 1a8e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Anderson, B F]]		[[Category: Anderson, B F]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]

OCA at 09:45, 22 December 2014

OCA — Mon, 22 Dec 2014 09:45:29 GMT

←Older revision		Revision as of 09:45, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [http://www.ebi.ac.uk/pdbsum/1a8e 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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [http://www.ebi.ac.uk/pdbsum/1a8e 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 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Anderson, B F.]]	+	[[Category: Anderson, B F]]
-	[[Category: Baker, E N.]]	+	[[Category: Baker, E N]]
-	[[Category: Baker, H.]]	+	[[Category: Baker, H]]
-	[[Category: Bewley, M.]]	+	[[Category: Bewley, M]]
-	[[Category: Brayer, G D.]]	+	[[Category: Brayer, G D]]
-	[[Category: Chen, J.]]	+	[[Category: Chen, J]]
-	[[Category: Luo, Y.]]	+	[[Category: Luo, Y]]
-	[[Category: Macgillivray, R T.A.]]	+	[[Category: Macgillivray, R T.A]]
-	[[Category: Mason, A B.]]	+	[[Category: Mason, A B]]
-	[[Category: Moore, S A.]]	+	[[Category: Moore, S A]]
-	[[Category: Murphy, M E.P.]]	+	[[Category: Murphy, M E.P]]
-	[[Category: Smith, C A.]]	+	[[Category: Smith, C A]]
-	[[Category: Wang, Y.]]	+	[[Category: Wang, Y]]
-	[[Category: Woodworth, R C.]]	+	[[Category: Woodworth, R C]]
	[[Category: Carbonate]]		[[Category: Carbonate]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]

OCA at 14:30, 29 September 2014

OCA — Mon, 29 Sep 2014 14:30:25 GMT

←Older revision		Revision as of 14:30, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1a8e~~\| ~~PDB~~=1a8e \| ~~SCENE~~= }}	+	==HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE==
-	===~~HUMAN SERUM TRANSFERRIN~~, ~~RECOMBINANT N~~-~~TERMINAL LOBE~~===	+	<StructureSection load='1a8e' size='340' side='right' caption='[[1a8e]], [[Resolution\|resolution]] 1.60Å' scene=''>
-	~~{{ABSTRACT_PUBMED_9609685}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1a8e]] is a 1 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=1A8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A8E FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>
		+	<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=1a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a8e RCSB], [http://www.ebi.ac.uk/pdbsum/1a8e 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/a8/1a8e_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 ==
		+	The N-lobe of human serum transferrin (hTF/2N) has been expressed in baby hamster kidney cells and crystallized in both orthorhombic (P212121) and tetragonal (P41212) space groups. Both crystal forms diffract to high resolution (1.6 and 1.8 A, respectively) and have been solved by molecular replacement. Subsequent refinement resulted in final models for the structure of hTF/2N that had crystallographic R-factors of 18.1 and 19.7% for the two crystal forms, respectively; these models represent the highest-resolution transferrin structures determined to date. The hTF/2N polypeptide has a folding pattern similar to those of other transferrins, including the presence of a deep cleft that contains the metal-binding site. In contrast to other transferrins, both crystal forms of hTF/2N display disorder at the iron-binding site; model building suggests that this disorder consists of alternative conformations of the synergistically bound carbonate anion, the side chain for Arg-124, and several solvent molecules. Subsequent refinement revealed that conformation A has an occupancy of 0.63-0. 65 and corresponds to the structure of the iron-binding site found in other transferrins. The alternative conformation B has an occupancy of 0.35-0.37; in this structure, the carbonate has rotated 30 degrees relative to the iron and the side chain for Arg-124 has moved to accommodate the new carbonate position. Several water molecules appear to stabilize the carbonate anion in the two conformations. These structures are consistent with the protonation of the carbonate and resulting partial removal of the anion from the metal; these events would occur prior to cleft opening and metal release.

-	~~==Disease==~~	+	Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release.,MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN Biochemistry. 1998 Jun 2;37(22):7919-28. PMID:9609685<ref>PMID:9609685</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==~~	+
-	~~[[1a8e]] is a 1 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=1A8E OCA].~~	+

	==See Also==		==See Also==
	*[[Transferrin\|Transferrin]]		*[[Transferrin\|Transferrin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:009609685</ref><ref group="xtra">PMID:011917145</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Anderson, B F.]]		[[Category: Anderson, B F.]]

OCA at 10:56, 24 March 2013

OCA — Sun, 24 Mar 2013 10:56:30 GMT

←Older revision		Revision as of 10:56, 24 March 2013
Line 1:		Line 1:
-	[[Image:1a8e.png\|left\|200px]]
-
	{{STRUCTURE_1a8e\| PDB=1a8e \| SCENE= }}		{{STRUCTURE_1a8e\| PDB=1a8e \| SCENE= }}
-
	===HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE===		===HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE===
		+	{{ABSTRACT_PUBMED_9609685}}

-	~~{{ABSTRACT_PUBMED_9609685}}~~	+	==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:009609685</ref><ref group="xtra">PMID:011917145</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009609685</ref><ref group="xtra">PMID:011917145</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Anderson, B F.]]		[[Category: Anderson, B F.]]

OCA at 09:56, 20 October 2012

OCA — Sat, 20 Oct 2012 09:56:30 GMT

←Older revision		Revision as of 09:56, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1a8e]] is a 1 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=1A8E OCA].	+	[[1a8e]] is a 1 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=1A8E OCA].

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