1n3y: Difference between revisions
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==Crystal structure of the alpha-X beta2 integrin I domain== | ==Crystal structure of the alpha-X beta2 integrin I domain== | ||
<StructureSection load='1n3y' size='340' side='right' caption='[[1n3y]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='1n3y' size='340' side='right'caption='[[1n3y]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1n3y]] 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=1N3Y OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1n3y]] 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=1N3Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N3Y FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITGAX OR CD11C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITGAX OR CD11C ([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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3y OCA], [http://pdbe.org/1n3y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n3y RCSB], [http://www.ebi.ac.uk/pdbsum/1n3y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n3y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1n3y" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1n3y" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Integrin 3D structures|Integrin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Hommel, U]] | [[Category: Hommel, U]] | ||
[[Category: Ostermeier, C]] | [[Category: Ostermeier, C]] | ||
Revision as of 11:44, 2 December 2020
Crystal structure of the alpha-X beta2 integrin I domainCrystal structure of the alpha-X beta2 integrin I domain
Structural highlights
Function[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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe integrin alpha X beta 2 (CD11c/CD18, p150,95) binds ligands through the I domain of the alpha X subunit. Ligands include the complement factor fragment iC3b, a key component in the innate immune defense, which, together with the expression of alpha X beta 2 on dendritic cells and on other leukocytes, suggests a role in the immune response. We now report the structure of the alpha X I domain resolved at 1.65 A by x-ray crystallography. To analyze structural requirements for ligand binding we made a mutation in the alpha X I domain C-terminal helix, which increased the affinity for iC3b approximately 200-fold to 2.4 microM compared with the wild-type domain affinity of approximately 400 microM. Gel permeation chromatography supported a conformational change between the wild-type and mutated domains. Conservation of allosteric regulation in the alpha X I domain points to the functional importance of this phenomenon. Structure and allosteric regulation of the alpha X beta 2 integrin I domain.,Vorup-Jensen T, Ostermeier C, Shimaoka M, Hommel U, Springer TA Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1873-8. Epub 2003 Jan 28. PMID:12554829[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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