5e6v - Revision history

OCA at 06:15, 5 July 2023

OCA — Wed, 05 Jul 2023 06:15:05 GMT

←Older revision		Revision as of 06:15, 5 July 2023
Line 3:		Line 3:
	<StructureSection load='5e6v' size='340' side='right'caption='[[5e6v]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='5e6v' size='340' side='right'caption='[[5e6v]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5e6v]] 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=5E6V OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5E6V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5e6v]] 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=5E6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E6V FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=FUL:BETA~~-~~L-FUCOSE'>FUL</scene>~~, ~~<scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~PCA~~:~~PYROGLUTAMIC+ACID~~'>~~PCA~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class="sblockDat">[[1yuk\|1yuk]]</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=5e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6v OCA], [https://pdbe.org/5e6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e6v RCSB], [https://www.ebi.ac.uk/pdbsum/5e6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6v ProSAT]</span></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">ITGB2, CD18, MFI7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=5e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6v OCA], [~~http~~://pdbe.org/5e6v PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5e6v RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5e6v PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6v ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Defects in ITGB2 are the cause of leukocyte adhesion deficiency type 1 (LAD1) [MIM:[~~http~~://omim.org/entry/116920 116920]]. LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.<ref>PMID:7509236</ref> <ref>PMID:1346613</ref> <ref>PMID:1968911</ref> <ref>PMID:1694220</ref> <ref>PMID:1590804</ref> <ref>PMID:1352501</ref> <ref>PMID:1347532</ref> <ref>PMID:7686755</ref> <ref>PMID:9884339</ref> <ref>PMID:20529581</ref> <ref>PMID:20549317</ref>	+	[https://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN] Defects in ITGB2 are the cause of leukocyte adhesion deficiency type 1 (LAD1) [MIM:[https://omim.org/entry/116920 116920]. LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.<ref>PMID:7509236</ref> <ref>PMID:1346613</ref> <ref>PMID:1968911</ref> <ref>PMID:1694220</ref> <ref>PMID:1590804</ref> <ref>PMID:1352501</ref> <ref>PMID:1347532</ref> <ref>PMID:7686755</ref> <ref>PMID:9884339</ref> <ref>PMID:20529581</ref> <ref>PMID:20549317</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.<ref>PMID:18587400</ref>	+	[https://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.<ref>PMID:18587400</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	Integrins are modular (alphabeta) heterodimeric proteins that mediate cell adhesion and convey signals across the plasma membrane. Interdomain motions play a key role in signal transduction by propagating structural changes through the molecule, thus controlling the activation state and adhesive properties of the ~~integrin. We expressed a soluble fragment~~ of ~~the human integrin beta2 subunit comprising the plexin~~-~~semaphorin~~-integrin ~~domain (PSI~~)~~/hybrid~~ domain/I-~~EGF1 fragment~~ and ~~present its crystal structure at 1.8~~-~~A resolution~~. The ~~structure reveals an elongated molecule with a rigid architecture stabilized by nine disulfide bridges. The PSI domain is located centrally and participates in the formation of extended interfaces~~ with the ~~hybrid~~ domain and I-~~EGF1 domains, respectively. The hybrid domain/PSI interface involves~~ the ~~burial~~ of ~~an Arg residue~~, and ~~contacts~~ between ~~PSI~~ and ~~I-EGF1 are mainly mediated by well conserved Arg and Trp residues~~. ~~Conservation of key interacting residues across the various~~ integrin ~~beta subunits sequences suggests that our structure represents a good model for~~ the ~~entire integrin family~~. ~~Superposition with~~ the ~~integrin beta3 receptor in its bent conformation suggests that~~ an ~~articulation point is present~~ at the ~~linkage~~ between ~~its I~~-~~EGF1~~ and I-~~EGF2 modules~~ and ~~underlines~~ the ~~importance~~ of ~~this region~~ for the ~~control of integrin-mediated cell adhesion~~.	+	High-resolution crystal structures of the headpiece of lymphocyte function-associated antigen-1 (integrin alphaLbeta2) reveal how the alphaI domain interacts with its platform formed by the alpha-subunit beta-propeller and beta-subunit betaI domains. The alphaLbeta2 structures compared with alphaXbeta2 structures show that the alphaI domain, tethered through its N-linker and a disulfide to a stable beta-ribbon pillar near the center of the platform, can undergo remarkable pivoting and tilting motions that appear buffered by N-glycan decorations that differ between alphaL and alphaX subunits. Rerefined beta2 integrin structures reveal details including pyroglutamic acid at the beta2 N terminus and bending within the EGF1 domain. Allostery is relayed to the alphaI domain by an internal ligand that binds to a pocket at the interface between the beta-propeller and betaI domains. Marked differences between the alphaL and alphaX subunit beta-propeller domains concentrate near the binding pocket and alphaI domain interfaces. Remarkably, movement in allostery in the betaI domain of specificity determining loop 1 (SDL1) causes concerted movement of SDL2 and thereby tightens the binding pocket for the internal ligand.

-	The ~~crystal structure of the plexin-semaphorin-integrin~~ domain~~/hybrid domain/I-EGF1 segment from~~ the ~~human integrin beta2 subunit at 1.8-A resolution~~.,~~Shi~~ M, ~~Sundramurthy K, Liu B, Tan SM, Law SK, Lescar J J Biol Chem~~. ~~2005 Aug 26~~;~~280~~(34):~~30586~~-93. Epub ~~2005 Jun 17~~. PMID:~~15965234~~<ref>PMID:~~15965234~~</ref>	+	Leukocyte integrin alphaLbeta2 headpiece structures: The alphaI domain, the pocket for the internal ligand, and concerted movements of its loops.,Sen M, Springer TA Proc Natl Acad Sci U S A. 2016 Mar 15;113(11):2940-5. doi:, 10.1073/pnas.1601379113. Epub 2016 Mar 2. PMID:26936951<ref>PMID:26936951</ref>

	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>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Sen, M]]	+	[[Category: Sen M]]
-	[[Category: Springer~~, T A]]~~	+	[[Category: Springer TA]]
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Lfa-1]]~~	+
-	~~[[Category: Lymphocyte function-associated antigen-1~~]]	+

OCA at 08:59, 4 December 2019

OCA — Wed, 04 Dec 2019 08:59:56 GMT

←Older revision		Revision as of 08:59, 4 December 2019
Line 1:		Line 1:

	==Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit==		==Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit==
-	<StructureSection load='5e6v' size='340' side='right' caption='[[5e6v]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='5e6v' size='340' side='right'caption='[[5e6v]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5e6v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6V FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5e6v]] 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=5E6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6V FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yuk\|1yuk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yuk\|1yuk]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ITGB2, CD18, MFI7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6v OCA], [http://pdbe.org/5e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6v RCSB], [http://www.ebi.ac.uk/pdbsum/5e6v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6v ProSAT]</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=5e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6v OCA], [http://pdbe.org/5e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6v RCSB], [http://www.ebi.ac.uk/pdbsum/5e6v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6v ProSAT]</span></td></tr>
	</table>		</table>
Line 22:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 5e6v" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5e6v" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Integrin 3D structures\|Integrin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Sen, M]]		[[Category: Sen, M]]
	[[Category: Springer, T A]]		[[Category: Springer, T A]]

OCA at 12:36, 6 November 2017

OCA — Mon, 06 Nov 2017 12:36:58 GMT

←Older revision		Revision as of 12:36, 6 November 2017
Line 22:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 5e6v" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5e6v" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Integrin\|Integrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:21, 27 September 2017

OCA — Wed, 27 Sep 2017 10:21:30 GMT

←Older revision		Revision as of 10:21, 27 September 2017
Line 22:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 5e6v" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5e6v" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Integrin\|Integrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:21, 15 March 2017

OCA — Wed, 15 Mar 2017 13:21:28 GMT

←Older revision		Revision as of 13:21, 15 March 2017
Line 7:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yuk\|1yuk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yuk\|1yuk]]</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=5e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6v OCA], [http://pdbe.org/5e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6v RCSB], [http://www.ebi.ac.uk/pdbsum/5e6v 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=5e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6v OCA], [http://pdbe.org/5e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6v RCSB], [http://www.ebi.ac.uk/pdbsum/5e6v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6v ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 15:		Line 15:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~High-resolution crystal structures~~ of the ~~headpiece~~ of ~~lymphocyte function~~-~~associated antigen~~-~~1 (~~integrin ~~alphaLbeta2~~) ~~reveal how the alphaI~~ domain ~~interacts with its platform formed by the alpha~~-~~subunit beta-propeller~~ and ~~beta~~-~~subunit betaI domains~~. The ~~alphaLbeta2 structures compared~~ with ~~alphaXbeta2 structures show that~~ the ~~alphaI~~ domain~~, tethered through its N-linker~~ and ~~a disulfide to a stable beta~~-~~ribbon pillar near~~ the ~~center~~ of ~~the platform~~, ~~can undergo remarkable pivoting~~ and ~~tilting motions that appear buffered by N-glycan decorations that differ~~ between ~~alphaL~~ and ~~alphaX subunits~~. ~~Rerefined beta2~~ integrin ~~structures reveal details including pyroglutamic acid at~~ the ~~beta2 N terminus and bending within the EGF1 domain~~. ~~Allostery is relayed to~~ the ~~alphaI domain by~~ an ~~internal ligand that binds to a pocket~~ at the ~~interface~~ between ~~the beta~~-~~propeller~~ and ~~betaI domains. Marked differences between the alphaL and alphaX subunit beta~~-~~propeller domains concentrate near the binding pocket~~ and ~~alphaI domain interfaces. Remarkably, movement in allostery in~~ the ~~betaI domain~~ of ~~specificity determining loop 1 (SDL1) causes concerted movement of SDL2 and thereby tightens the binding pocket~~ for the ~~internal ligand~~.	+	Integrins are modular (alphabeta) heterodimeric proteins that mediate cell adhesion and convey signals across the plasma membrane. Interdomain motions play a key role in signal transduction by propagating structural changes through the molecule, thus controlling the activation state and adhesive properties of the integrin. We expressed a soluble fragment of the human integrin beta2 subunit comprising the plexin-semaphorin-integrin domain (PSI)/hybrid domain/I-EGF1 fragment and present its crystal structure at 1.8-A resolution. The structure reveals an elongated molecule with a rigid architecture stabilized by nine disulfide bridges. The PSI domain is located centrally and participates in the formation of extended interfaces with the hybrid domain and I-EGF1 domains, respectively. The hybrid domain/PSI interface involves the burial of an Arg residue, and contacts between PSI and I-EGF1 are mainly mediated by well conserved Arg and Trp residues. Conservation of key interacting residues across the various integrin beta subunits sequences suggests that our structure represents a good model for the entire integrin family. Superposition with the integrin beta3 receptor in its bent conformation suggests that an articulation point is present at the linkage between its I-EGF1 and I-EGF2 modules and underlines the importance of this region for the control of integrin-mediated cell adhesion.

-	~~Leukocyte integrin alphaLbeta2 headpiece structures:~~ The ~~alphaI~~ domain~~, the pocket for~~ the ~~internal ligand, and concerted movements of its loops~~.,~~Sen~~ M, ~~Springer TA Proc Natl Acad Sci U S A~~. ~~2016 Mar 15~~;~~113~~(11):~~2940~~-~~5. doi:, 10.1073/pnas.1601379113~~. Epub ~~2016 Mar 2~~. PMID:~~26936951~~<ref>PMID:~~26936951~~</ref>	+	The crystal structure of the plexin-semaphorin-integrin domain/hybrid domain/I-EGF1 segment from the human integrin beta2 subunit at 1.8-A resolution.,Shi M, Sundramurthy K, Liu B, Tan SM, Law SK, Lescar J J Biol Chem. 2005 Aug 26;280(34):30586-93. Epub 2005 Jun 17. PMID:15965234<ref>PMID:15965234</ref>

	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>

OCA at 19:26, 10 May 2016

OCA — Tue, 10 May 2016 19:26:32 GMT

←Older revision		Revision as of 19:26, 10 May 2016
Line 13:		Line 13:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.<ref>PMID:18587400</ref>		[[http://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.<ref>PMID:18587400</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	High-resolution crystal structures of the headpiece of lymphocyte function-associated antigen-1 (integrin alphaLbeta2) reveal how the alphaI domain interacts with its platform formed by the alpha-subunit beta-propeller and beta-subunit betaI domains. The alphaLbeta2 structures compared with alphaXbeta2 structures show that the alphaI domain, tethered through its N-linker and a disulfide to a stable beta-ribbon pillar near the center of the platform, can undergo remarkable pivoting and tilting motions that appear buffered by N-glycan decorations that differ between alphaL and alphaX subunits. Rerefined beta2 integrin structures reveal details including pyroglutamic acid at the beta2 N terminus and bending within the EGF1 domain. Allostery is relayed to the alphaI domain by an internal ligand that binds to a pocket at the interface between the beta-propeller and betaI domains. Marked differences between the alphaL and alphaX subunit beta-propeller domains concentrate near the binding pocket and alphaI domain interfaces. Remarkably, movement in allostery in the betaI domain of specificity determining loop 1 (SDL1) causes concerted movement of SDL2 and thereby tightens the binding pocket for the internal ligand.
		+
		+	Leukocyte integrin alphaLbeta2 headpiece structures: The alphaI domain, the pocket for the internal ligand, and concerted movements of its loops.,Sen M, Springer TA Proc Natl Acad Sci U S A. 2016 Mar 15;113(11):2940-5. doi:, 10.1073/pnas.1601379113. Epub 2016 Mar 2. PMID:26936951<ref>PMID:26936951</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5e6v" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:24, 2 March 2016

OCA — Wed, 02 Mar 2016 15:24:40 GMT

←Older revision		Revision as of 15:24, 2 March 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 5e6v is ON HOLD~~	+	==Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit==
-		+	<StructureSection load='5e6v' size='340' side='right' caption='[[5e6v]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~Authors: Sen, M., Springer, T.A.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5e6v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6V FirstGlance]. <br>
-	~~Description:~~ Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
-	[[~~Category~~: ~~Springer~~, T.A]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yuk\|1yuk]]</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=5e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6v OCA], [http://pdbe.org/5e6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6v RCSB], [http://www.ebi.ac.uk/pdbsum/5e6v PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Defects in ITGB2 are the cause of leukocyte adhesion deficiency type 1 (LAD1) [MIM:[http://omim.org/entry/116920 116920]]. LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.<ref>PMID:7509236</ref> <ref>PMID:1346613</ref> <ref>PMID:1968911</ref> <ref>PMID:1694220</ref> <ref>PMID:1590804</ref> <ref>PMID:1352501</ref> <ref>PMID:1347532</ref> <ref>PMID:7686755</ref> <ref>PMID:9884339</ref> <ref>PMID:20529581</ref> <ref>PMID:20549317</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.<ref>PMID:18587400</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Sen, M]]		[[Category: Sen, M]]
		+	[[Category: Springer, T A]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Lfa-1]]
		+	[[Category: Lymphocyte function-associated antigen-1]]

OCA at 11:40, 16 December 2015

OCA — Wed, 16 Dec 2015 11:40:59 GMT

←Older revision		Revision as of 11:40, 16 December 2015
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	Description: Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit		Description: Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Sen, M]]
	[[Category: Springer, T.A]]		[[Category: Springer, T.A]]
		+	[[Category: Sen, M]]

OCA: Protected "5e6v" [edit=sysop:move=sysop]

OCA — Thu, 22 Oct 2015 04:25:27 GMT

Protected "5e6v" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:25, 22 October 2015

OCA: New page: '''Unreleased structure''' The entry 5e6v is ON HOLD Authors: Sen, M., Springer, T.A. Description: Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybri...

OCA — Thu, 22 Oct 2015 04:25:26 GMT

New page: '''Unreleased structure''' The entry 5e6v is ON HOLD Authors: Sen, M., Springer, T.A. Description: Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybri...

New page

'''Unreleased structure'''

The entry 5e6v is ON HOLD

Authors: Sen, M., Springer, T.A.

Description: Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit
[[Category: Unreleased Structures]]
[[Category: Sen, M]]
[[Category: Springer, T.A]]