1iam: Difference between revisions
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New page: left|200px<br /> <applet load="1iam" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iam, resolution 2.10Å" /> '''STRUCTURE OF THE TW... |
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== | ==STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1== | ||
The normal function of human intercellular adhesion molecule-1 (ICAM-1) is | <StructureSection load='1iam' size='340' side='right'caption='[[1iam]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1iam]] 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=1IAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAM 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]] 2.1Å</td></tr> | |||
<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'>[https://proteopedia.org/fgij/fg.htm?mol=1iam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iam OCA], [https://pdbe.org/1iam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iam RCSB], [https://www.ebi.ac.uk/pdbsum/1iam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iam ProSAT]</span></td></tr> | |||
</table> | |||
== 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 == | |||
[[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/ia/1iam_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=1iam ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The normal function of human intercellular adhesion molecule-1 (ICAM-1) is to provide adhesion between endothelial cells and leukocytes after injury or stress. ICAM-1 binds to leukocyte function-associated antigen (LFA-1) or macrophage-1 antigen (Mac-1). However, ICAM-1 is also used as a receptor by the major group of human rhinoviruses and is a catalyst for the subsequent viral uncoating during cell entry. The three-dimensional atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1 has been determined to 2.2-A resolution and fitted into a cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex. Rhinovirus attachment is confined to the BC, CD, DE, and FG loops of the amino-terminal Ig-like domain (D1) at the end distal to the cellular membrane. The loops are considerably different in structure to those of human ICAM-2 or murine ICAM-1, which do not bind rhinoviruses. There are extensive charge interactions between ICAM-1 and human rhinoviruses, which are mostly conserved in both major and minor receptor groups of rhinoviruses. The interaction of ICAMs with LFA-1 is known to be mediated by a divalent cation bound to the insertion (I)-domain on the alpha chain of LFA-1 and the carboxyl group of a conserved glutamic acid residue on ICAMs. Domain D1 has been docked with the known structure of the I-domain. The resultant model is consistent with mutational data and provides a structural framework for the adhesion between these molecules. | |||
The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand.,Bella J, Kolatkar PR, Marlor CW, Greve JM, Rossmann MG Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4140-5. PMID:9539703<ref>PMID:9539703</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1iam" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Intercellular adhesion molecule|Intercellular adhesion molecule]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bella | [[Category: Bella J]] | ||
[[Category: Greve | [[Category: Greve JM]] | ||
[[Category: Kolatkar | [[Category: Kolatkar PR]] | ||
[[Category: Marlor | [[Category: Marlor C]] | ||
[[Category: Rossmann | [[Category: Rossmann MG]] | ||
Latest revision as of 06:45, 30 October 2024
STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1
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