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1n3y
From Proteopedia
(Difference between revisions)
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<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 [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1n3y]] 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=1N3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N3Y FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</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=1n3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3y OCA], [https://pdbe.org/1n3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n3y RCSB], [https://www.ebi.ac.uk/pdbsum/1n3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n3y 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=1n3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3y OCA], [https://pdbe.org/1n3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n3y RCSB], [https://www.ebi.ac.uk/pdbsum/1n3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n3y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1n3y 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=1n3y ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The 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<ref>PMID:12554829</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1n3y" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Integrin 3D structures|Integrin 3D structures]] | *[[Integrin 3D structures|Integrin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hommel | + | [[Category: Hommel U]] |
| - | [[Category: Ostermeier | + | [[Category: Ostermeier C]] |
| - | [[Category: Shimaoka | + | [[Category: Shimaoka M]] |
| - | [[Category: Springer | + | [[Category: Springer TA]] |
| - | [[Category: Vorup-Jensen | + | [[Category: Vorup-Jensen T]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the alpha-X beta2 integrin I domain
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