2o7u - Revision history

OCA at 10:33, 30 August 2023

2023-08-30T10:33:04Z

← Older revision		Revision as of 10:33, 30 August 2023
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	<StructureSection load='2o7u' size='340' side='right'caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='2o7u' size='340' side='right'caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7U FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7U 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]] 2.8Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height~~: ~~3em;~~'>~~[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]~~</~~div~~></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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [https://pdbe.org/2o7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [https://www.ebi.ac.uk/pdbsum/2o7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7u 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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [https://pdbe.org/2o7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [https://www.ebi.ac.uk/pdbsum/2o7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7u 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]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Baker~~, E N~~]]		[[Category: Baker EN]]
	[[Category: Baker~~, H M~~]]		[[Category: Baker HM]]
	[[Category: Mason~~, A B~~]]		[[Category: Mason AB]]
	[[Category: Nurizzo, D]]		[[Category: Nurizzo D]]
	~~[[Category: Dilysine pair]]~~
	~~[[Category: Human transferrin]]~~
	~~[[Category: Iron binding protein]]~~
	~~[[Category: Metal transport~~]]

OCA at 16:02, 8 June 2021

2021-06-08T16:02:28Z

← Older revision		Revision as of 16:02, 8 June 2021
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	<StructureSection load='2o7u' size='340' side='right'caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='2o7u' size='340' side='right'caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2O7U FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7U 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</div></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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [~~http~~://pdbe.org/2o7u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2o7u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7u 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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [https://pdbe.org/2o7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [https://www.ebi.ac.uk/pdbsum/2o7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7u 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]]
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	==See Also==		==See Also==
	*[[Transferrin\|Transferrin]]		*[[Transferrin 3D structures\|Transferrin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:46, 31 July 2019

2019-07-31T07:46:18Z

← Older revision		Revision as of 07:46, 31 July 2019
Line 1:		Line 1:

	==Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin==		==Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin==
	<StructureSection load='2o7u' size='340' side='right' caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='2o7u' size='340' side='right'caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7U FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7U FirstGlance]. <br>
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7u_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7u_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 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 2o7u" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2o7u" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]
	[[Category: Baker, H M]]		[[Category: Baker, H M]]

OCA at 08:53, 18 October 2017

2017-10-18T08:53:37Z

← Older revision		Revision as of 08:53, 18 October 2017
Line 1:		Line 1:

	==Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin==		==Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin==
	<StructureSection load='2o7u' size='340' side='right' caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='2o7u' size='340' side='right' caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>
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	</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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [http://pdbe.org/2o7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [http://www.ebi.ac.uk/pdbsum/2o7u 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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [http://pdbe.org/2o7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [http://www.ebi.ac.uk/pdbsum/2o7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7u ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	</div>		</div>
	<div class="pdbe-citations 2o7u" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2o7u" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:06, 8 February 2016

2016-02-08T08:06:52Z

← Older revision		Revision as of 08:06, 8 February 2016
Line 19:		Line 19:
	<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=2o7u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 09:33, 10 September 2015

2015-09-10T09:33:15Z

← Older revision		Revision as of 09:33, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2o7u' size='340' side='right' caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='2o7u' size='340' side='right' caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7U FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7U 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [http://www.ebi.ac.uk/pdbsum/2o7u 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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [http://pdbe.org/2o7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [http://www.ebi.ac.uk/pdbsum/2o7u PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 2o7u" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Baker, E N]]		[[Category: Baker, E N]]
	[[Category: Baker, H M]]		[[Category: Baker, H M]]

OCA at 18:17, 19 January 2015

2015-01-19T18:17:13Z

← Older revision		Revision as of 18:17, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7U FirstGlance]. <br>		<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7U 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>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [http://www.ebi.ac.uk/pdbsum/2o7u 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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [http://www.ebi.ac.uk/pdbsum/2o7u 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>
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	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Baker, E N.]]		[[Category: Baker, E N]]
	[[Category: Baker, H M.]]		[[Category: Baker, H M]]
	[[Category: Mason, A B.]]		[[Category: Mason, A B]]
	[[Category: Nurizzo, D.]]		[[Category: Nurizzo, D]]
	[[Category: Dilysine pair]]		[[Category: Dilysine pair]]
	[[Category: Human transferrin]]		[[Category: Human transferrin]]
	[[Category: Iron binding protein]]		[[Category: Iron binding protein]]
	[[Category: Metal transport]]		[[Category: Metal transport]]

OCA at 20:11, 30 September 2014

2014-09-30T20:11:31Z

← Older revision		Revision as of 20:11, 30 September 2014
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	~~{{STRUCTURE_2o7u\| PDB=2o7u \| SCENE= }}~~		==Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin==
	===Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin===		<StructureSection load='2o7u' size='340' side='right' caption='[[2o7u]], [[Resolution\|resolution]] 2.80Å' scene=''>
	~~{{ABSTRACT_PUBMED_17327678}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2o7u]] is a 9 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=2O7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7U FirstGlance]. <br>
	==Disease==		</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>
	[[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>		<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a8e\|1a8e]], [[1fqf\|1fqf]], [[1fqe\|1fqe]], [[1eh3\|1eh3]], [[1h43\|1h43]], [[1h45\|1h45]], [[2o84\|2o84]]</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=2o7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o7u RCSB], [http://www.ebi.ac.uk/pdbsum/2o7u 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/o7/2o7u_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 ==
			Iron uptake by humans depends on the ability of the serum protein transferrin (Tf) to bind iron as Fe(3+) with high affinity but reversibly. Iron release into cells occurs through receptor-mediated endocytosis, aided by the lower endosomal pH of about 5.5. The protonation of a hydrogen-bonded pair of lysines, Lys206 and Lys296, adjacent to the N-lobe iron site of Tf has been proposed to create a repulsive interaction that stimulates domain opening and iron release. The crystal structures of two mutants, K206E (in which Lys206 is mutated to Glu) and K206E/K296E (in which both lysines are mutated to Glu), have been determined. The K206E structure (2.6 A resolution; R = 0.213, R(free) = 0.269) shows that a salt bridge is formed between Glu206 and Lys296, thus explaining the drastically slower iron release by this mutant. The K206E/K296E double-mutant structure (2.8 A resolution; R = 0.232, R(free) = 0.259) shows that the Glu296 side chain moves away from Glu206, easing any repulsive interaction and instead interacting with the iron ligand His249. The evident conformational flexibility is consistent with an alternative model for the operation of the dilysine pair in iron release in which it facilitates concerted proton transfer to the tyrosine ligand Tyr188 as one step in the weakening of iron binding.

	~~==Function==~~		Structures of two mutants that probe the role in iron release of the dilysine pair in the N-lobe of human transferrin.,Baker HM, Nurizzo D, Mason AB, Baker EN Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):408-14. Epub 2007, Feb 21. PMID:17327678<ref>PMID:17327678</ref>
	~~[[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==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[2o7u]] is~~ a ~~9 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=2O7U OCA].~~		</div>

	==See Also==		==See Also==
	*[[Transferrin\|Transferrin]]		*[[Transferrin\|Transferrin]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:017327678</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Baker, E N.]]		[[Category: Baker, E N.]]

OCA at 07:01, 25 March 2013

2013-03-25T07:01:15Z

← Older revision		Revision as of 07:01, 25 March 2013
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	~~[[Image:2o7u.png\|left\|200px]]~~

	{{STRUCTURE_2o7u\| PDB=2o7u \| SCENE= }}		{{STRUCTURE_2o7u\| PDB=2o7u \| SCENE= }}
			===Crystal structure of K206E/K296E mutant of the N-terminal half molecule of human transferrin===
			{{ABSTRACT_PUBMED_17327678}}

	===~~Crystal structure of K206E~~/~~K296E mutant of~~ the ~~N-terminal half molecule~~ of ~~human transferrin===~~		==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>

	~~{{ABSTRACT_PUBMED_17327678}}~~		==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:017327678</ref><references group="xtra"/>		<ref group="xtra">PMID:017327678</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Baker, E N.]]		[[Category: Baker, E N.]]

OCA at 09:29, 20 October 2012

2012-10-20T09:29:40Z

← Older revision		Revision as of 09:29, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[2o7u]] is a 9 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=2O7U OCA].		[[2o7u]] is a 9 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=2O7U OCA].

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