1t0p
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1t0p.png|left|200px]] | ||
- | < | + | ==Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A== |
- | + | <StructureSection load='1t0p' size='340' side='right'caption='[[1t0p]], [[Resolution|resolution]] 1.66Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1t0p]] 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=1T0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0P 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]] 1.66Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1t0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0p OCA], [https://pdbe.org/1t0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0p RCSB], [https://www.ebi.ac.uk/pdbsum/1t0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0p ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ITAL_HUMAN ITAL_HUMAN] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes. | ||
+ | == 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/t0/1t0p_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1t0p ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Within the Ig superfamily (IgSF), intercellular adhesion molecules (ICAMs) form a subfamily that binds the leukocyte integrin alphaLbeta2. We report a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the inserted domain, the ligand-binding domain of alphaLbeta2. This high-resolution structure and comparisons among ICAM subfamily members establish that the binding of ICAM-3 D1 onto the inserted domain represents a common docking mode for ICAM subfamily members. The markedly different off-rates of ICAM-1, -2, and -3 appear to be determined by the hydrophobicity of residues that surround a metal coordination bond in the alphaLbeta2-binding interfaces. Variation in composition of glycans on the periphery of the interfaces influences on-rate. | ||
- | + | An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2.,Song G, Yang Y, Liu JH, Casasnovas JM, Shimaoka M, Springer TA, Wang JH Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3366-71. Epub 2005 Feb 22. PMID:15728350<ref>PMID:15728350</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1t0p" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Integrin 3D structures|Integrin 3D structures]] | |
- | + | *[[Intercellular adhesion molecule|Intercellular adhesion molecule]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
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- | + | ||
- | == | + | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Liu | + | [[Category: Liu JH]] |
- | [[Category: Shimaoko | + | [[Category: Shimaoko M]] |
- | [[Category: Song | + | [[Category: Song G]] |
- | [[Category: Springer | + | [[Category: Springer TA]] |
- | [[Category: Wang | + | [[Category: Wang JH]] |
- | [[Category: Yang | + | [[Category: Yang YT]] |
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Current revision
Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A
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Categories: Homo sapiens | Large Structures | Liu JH | Shimaoko M | Song G | Springer TA | Wang JH | Yang YT