1ibe - Revision history

OCA at 07:33, 7 February 2024

OCA — Wed, 07 Feb 2024 07:33:49 GMT

←Older revision		Revision as of 07:33, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.8Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [https://pdbe.org/1ibe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [https://www.ebi.ac.uk/pdbsum/1ibe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibe 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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [https://pdbe.org/1ibe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [https://www.ebi.ac.uk/pdbsum/1ibe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE~~]] Involved in oxygen transport from the lung to the various peripheral tissues. [[https://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]~~] Involved in oxygen transport from the lung to the various peripheral tissues.	+	[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</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=1ibe 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=1ibe ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Co-operative oxygen binding by the vertebrate haemoglobins arises from an equilibrium between a quaternary structure with low affinity (T), favoured in the absence of ligand, and a high affinity form (R) adopted by the fully ligated protein. While R state haemoglobin has an oxygen affinity close to that of isolated subunits, the affinity of the T state is roughly 300-fold lower. The mechanism by which the T state restrains ligand binding, and the pathway of the quaternary transition, have been largely revealed by detailed crystallographic analyses of a number of haemoglobin molecules in the equilibrium states, as well as intermediate forms of the T state including partially ligated species. The ligation intermediates of the R state, however, have not been as well characterized structurally. We report here the crystal structure of one such intermediate species, namely, horse deoxyhaemoglobin in the R state, at 1.8 A resolution. While ligand binding in the T state may result in unfavourable stereochemistry in and around the haem-ligand complex, the more plastic R structure appears to accommodate equally well both liganded and ligand-free haem. Loss of ligand at the R state haem results in movements of the haem and shifts of the FG corners, which form characteristic intersubunit contacts that distinguish the quaternary states. The shifts are comparable in magnitude to the corresponding movements associated with de-ligation in the T state, although they differ in direction. These and other differences illustrate how the structural changes in the haem pocket are communicated to the subunit interfaces and how the movements that can occur in the R state may be impeded in the T state.
-
-	The crystal structure of horse deoxyhaemoglobin trapped in the high-affinity (R) state.,Wilson J, Phillips K, Luisi B J Mol Biol. 1996 Dec 13;264(4):743-56. PMID:8980683<ref>PMID:8980683</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1ibe" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Hemoglobin 3D structures\|Hemoglobin 3D structures]]		*[[Hemoglobin 3D structures\|Hemoglobin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Luisi, B]]	+	[[Category: Luisi B]]
-	[[Category: Phillips, K]]	+	[[Category: Phillips K]]
-	[[Category: Wilson, J]]	+	[[Category: Wilson J]]
-	~~[[Category: Erythrocyte]]~~	+
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Oxygen transport]]~~	+
-	~~[[Category: Respiratory protein~~]]	+

OCA at 09:18, 29 September 2021

OCA — Wed, 29 Sep 2021 09:18:55 GMT

←Older revision		Revision as of 09:18, 29 September 2021
Line 3:		Line 3:
	<StructureSection load='1ibe' size='340' side='right'caption='[[1ibe]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1ibe' size='340' side='right'caption='[[1ibe]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1IBE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [~~http~~://pdbe.org/1ibe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ibe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibe 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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [https://pdbe.org/1ibe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [https://www.ebi.ac.uk/pdbsum/1ibe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. [[~~http~~://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues.	+	[[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. [[https://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:56, 25 December 2019

OCA — Wed, 25 Dec 2019 13:56:56 GMT

←Older revision		Revision as of 13:56, 25 December 2019
Line 1:		Line 1:

	==DEOXY-HAEMOGLOBIN TRAPPED IN THE HIGH-AFFINITY (R) STATE==		==DEOXY-HAEMOGLOBIN TRAPPED IN THE HIGH-AFFINITY (R) STATE==
-	<StructureSection load='1ibe' size='340' side='right' caption='[[1ibe]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1ibe' size='340' side='right'caption='[[1ibe]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
		+	[[Category: Large Structures]]
	[[Category: Luisi, B]]		[[Category: Luisi, B]]
	[[Category: Phillips, K]]		[[Category: Phillips, K]]

OCA at 09:18, 10 January 2018

OCA — Wed, 10 Jan 2018 09:18:40 GMT

←Older revision		Revision as of 09:18, 10 January 2018
Line 1:		Line 1:
		+
	==DEOXY-HAEMOGLOBIN TRAPPED IN THE HIGH-AFFINITY (R) STATE==		==DEOXY-HAEMOGLOBIN TRAPPED IN THE HIGH-AFFINITY (R) STATE==
	<StructureSection load='1ibe' size='340' side='right' caption='[[1ibe]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1ibe' size='340' side='right' caption='[[1ibe]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [http://pdbe.org/1ibe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [http://www.ebi.ac.uk/pdbsum/1ibe 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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [http://pdbe.org/1ibe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [http://www.ebi.ac.uk/pdbsum/1ibe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/1ibe_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/1ibe_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>

OCA at 02:56, 7 February 2016

OCA — Sun, 07 Feb 2016 02:56:03 GMT

←Older revision		Revision as of 02:56, 7 February 2016
Line 16:		Line 16:
	<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=1ibe ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:59, 9 September 2015

OCA — Wed, 09 Sep 2015 20:59:19 GMT

←Older revision		Revision as of 20:59, 9 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [http://www.ebi.ac.uk/pdbsum/1ibe 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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [http://pdbe.org/1ibe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [http://www.ebi.ac.uk/pdbsum/1ibe PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1ibe" style="background-color:#fffaf0;"></div>

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

OCA at 07:17, 24 December 2014

OCA — Wed, 24 Dec 2014 07:17:13 GMT

←Older revision		Revision as of 07:17, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [http://www.ebi.ac.uk/pdbsum/1ibe 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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [http://www.ebi.ac.uk/pdbsum/1ibe PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
-	[[Category: Luisi, B.]]	+	[[Category: Luisi, B]]
-	[[Category: Phillips, K.]]	+	[[Category: Phillips, K]]
-	[[Category: Wilson, J.]]	+	[[Category: Wilson, J]]
	[[Category: Erythrocyte]]		[[Category: Erythrocyte]]
	[[Category: Heme]]		[[Category: Heme]]
	[[Category: Oxygen transport]]		[[Category: Oxygen transport]]
	[[Category: Respiratory protein]]		[[Category: Respiratory protein]]

OCA at 08:46, 28 September 2014

OCA — Sun, 28 Sep 2014 08:46:42 GMT

←Older revision		Revision as of 08:46, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1ibe.~~png\|left~~\|200px]]	+	==DEOXY-HAEMOGLOBIN TRAPPED IN THE HIGH-AFFINITY (R) STATE==
		+	<StructureSection load='1ibe' size='340' side='right' caption='[[1ibe]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBE FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1ibe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ibe RCSB], [http://www.ebi.ac.uk/pdbsum/1ibe PDBsum]</span></td></tr>
		+	<table>
		+	== 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/ib/1ibe_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 ==
		+	Co-operative oxygen binding by the vertebrate haemoglobins arises from an equilibrium between a quaternary structure with low affinity (T), favoured in the absence of ligand, and a high affinity form (R) adopted by the fully ligated protein. While R state haemoglobin has an oxygen affinity close to that of isolated subunits, the affinity of the T state is roughly 300-fold lower. The mechanism by which the T state restrains ligand binding, and the pathway of the quaternary transition, have been largely revealed by detailed crystallographic analyses of a number of haemoglobin molecules in the equilibrium states, as well as intermediate forms of the T state including partially ligated species. The ligation intermediates of the R state, however, have not been as well characterized structurally. We report here the crystal structure of one such intermediate species, namely, horse deoxyhaemoglobin in the R state, at 1.8 A resolution. While ligand binding in the T state may result in unfavourable stereochemistry in and around the haem-ligand complex, the more plastic R structure appears to accommodate equally well both liganded and ligand-free haem. Loss of ligand at the R state haem results in movements of the haem and shifts of the FG corners, which form characteristic intersubunit contacts that distinguish the quaternary states. The shifts are comparable in magnitude to the corresponding movements associated with de-ligation in the T state, although they differ in direction. These and other differences illustrate how the structural changes in the haem pocket are communicated to the subunit interfaces and how the movements that can occur in the R state may be impeded in the T state.

-	~~{{STRUCTURE_1ibe\| PDB=1ibe \| SCENE= }}~~	+	The crystal structure of horse deoxyhaemoglobin trapped in the high-affinity (R) state.,Wilson J, Phillips K, Luisi B J Mol Biol. 1996 Dec 13;264(4):743-56. PMID:8980683<ref>PMID:8980683</ref>

-	~~===DEOXY-HAEMOGLOBIN TRAPPED IN THE HIGH-AFFINITY (R) STATE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8980683}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1ibe]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Equus_caballus Equus caballus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA].~~	+

	==See Also==		==See Also==
-	*[[Hemoglobin\|Hemoglobin]]	+	*[[Hemoglobin 3D structures\|Hemoglobin 3D structures]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008980683<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
	[[Category: Luisi, B.]]		[[Category: Luisi, B.]]

OCA at 05:24, 20 October 2012

OCA — Sat, 20 Oct 2012 05:24:04 GMT

←Older revision		Revision as of 05:24, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1ibe]] is a 2 chain structure ~~of [[Hemoglobin]]~~ with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA].	+	[[1ibe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBE OCA].

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

OCA: Protected "1ibe" [edit=sysop:move=sysop]

OCA — Wed, 25 Jul 2012 09:55:20 GMT

Protected "1ibe" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:55, 25 July 2012