4neh: Difference between revisions
New page: '''Unreleased structure''' The entry 4neh is ON HOLD Authors: Sen, M., Yuki, K., Springer, T.A. Description: An internal ligand-bound, metastable state of a leukocyte integrin, aXb2 |
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The | ==An internal ligand-bound, metastable state of a leukocyte integrin, aXb2== | ||
<StructureSection load='4neh' size='340' side='right'caption='[[4neh]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4neh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NEH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7505Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4neh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4neh OCA], [https://pdbe.org/4neh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4neh RCSB], [https://www.ebi.ac.uk/pdbsum/4neh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4neh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ITAX_HUMAN ITAX_HUMAN] Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
How is massive conformational change in integrins achieved on a rapid timescale? We report crystal structures of a metastable, putative transition state of integrin alphaXbeta2. The alphaXbeta2 ectodomain is bent; however, a lattice contact stabilizes its ligand-binding alphaI domain in a high affinity, open conformation. Much of the alphaI alpha7 helix unwinds, loses contact with the alphaI domain, and reshapes to form an internal ligand that binds to the interface between the beta propeller and betaI domains. Lift-off of the alphaI domain above this platform enables a range of extensional and rotational motions without precedent in allosteric machines. Movements of secondary structure elements in the beta2 betaI domain occur in an order different than in beta3 integrins, showing that integrin beta subunits can be specialized to assume different intermediate states between closed and open. Mutations demonstrate that the structure trapped here is metastable and can enable rapid equilibration between bent and extended-open integrin conformations and up-regulation of leukocyte adhesiveness. | |||
An internal ligand-bound, metastable state of a leukocyte integrin, alphaXbeta2.,Sen M, Yuki K, Springer TA J Cell Biol. 2013 Nov 25;203(4):629-42. doi: 10.1083/jcb.201308083. PMID:24385486<ref>PMID:24385486</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4neh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Integrin 3D structures|Integrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Sen M]] | |||
[[Category: Springer TA]] | |||
[[Category: Yuki K]] | |||
Latest revision as of 19:55, 20 September 2023
An internal ligand-bound, metastable state of a leukocyte integrin, aXb2An internal ligand-bound, metastable state of a leukocyte integrin, aXb2
Structural highlights
FunctionITAX_HUMAN Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis. Publication Abstract from PubMedHow is massive conformational change in integrins achieved on a rapid timescale? We report crystal structures of a metastable, putative transition state of integrin alphaXbeta2. The alphaXbeta2 ectodomain is bent; however, a lattice contact stabilizes its ligand-binding alphaI domain in a high affinity, open conformation. Much of the alphaI alpha7 helix unwinds, loses contact with the alphaI domain, and reshapes to form an internal ligand that binds to the interface between the beta propeller and betaI domains. Lift-off of the alphaI domain above this platform enables a range of extensional and rotational motions without precedent in allosteric machines. Movements of secondary structure elements in the beta2 betaI domain occur in an order different than in beta3 integrins, showing that integrin beta subunits can be specialized to assume different intermediate states between closed and open. Mutations demonstrate that the structure trapped here is metastable and can enable rapid equilibration between bent and extended-open integrin conformations and up-regulation of leukocyte adhesiveness. An internal ligand-bound, metastable state of a leukocyte integrin, alphaXbeta2.,Sen M, Yuki K, Springer TA J Cell Biol. 2013 Nov 25;203(4):629-42. doi: 10.1083/jcb.201308083. PMID:24385486[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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