1p53
From Proteopedia
(Difference between revisions)
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<StructureSection load='1p53' size='340' side='right'caption='[[1p53]], [[Resolution|resolution]] 3.06Å' scene=''> | <StructureSection load='1p53' size='340' side='right'caption='[[1p53]], [[Resolution|resolution]] 3.06Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1p53]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1p53]] 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=1P53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P53 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]] 3.06Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p53 OCA], [https://pdbe.org/1p53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p53 RCSB], [https://www.ebi.ac.uk/pdbsum/1p53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p53 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ICAM1_HUMAN ICAM1_HUMAN] ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus.<ref>PMID:2538243</ref> <ref>PMID:1968231</ref> <ref>PMID:11173916</ref> <ref>PMID:17875742</ref> |
== 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=1p53 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=1p53 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We have determined the 3.0 A crystal structure of the three C-terminal domains 3-5 (D3-D5) of ICAM-1. Combined with the previously known N-terminal two-domain structure (D1D2), a model of an entire ICAM-1 extracellular fragment has been constructed. This model should represent a general architecture of other ICAM family members, particularly ICAM-3 and ICAM-5. The observed intimate dimerization interaction at D4 and a stiff D4-D5 stem-like architecture provide a good structural explanation for the existence of preformed ICAM-1 cis dimers on the cell membrane. Together with another dimerization interface at D1, a band-like one-dimensional linear cluster of ICAM-1 on an antigen-presenting cell (APC) surface can be envisioned, which might explain the formation of an immunological synapse between an activated T cell and APC which is critical for T cell receptor signaling. | ||
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| - | Structural basis for dimerization of ICAM-1 on the cell surface.,Yang Y, Jun CD, Liu JH, Zhang R, Joachimiak A, Springer TA, Wang JH Mol Cell. 2004 Apr 23;14(2):269-76. PMID:15099525<ref>PMID:15099525</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1p53" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Jochimiak | + | [[Category: Jochimiak A]] |
| - | [[Category: Jun | + | [[Category: Jun CD]] |
| - | [[Category: Liu | + | [[Category: Liu JH]] |
| - | [[Category: Springer | + | [[Category: Springer TA]] |
| - | [[Category: Wang | + | [[Category: Wang JH]] |
| - | [[Category: Yang | + | [[Category: Yang Y]] |
| - | [[Category: Zhang | + | [[Category: Zhang R]] |
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Revision as of 05:52, 17 April 2024
The Crystal Structure of ICAM-1 D3-D5 fragment
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Categories: Homo sapiens | Large Structures | Jochimiak A | Jun CD | Liu JH | Springer TA | Wang JH | Yang Y | Zhang R
