1ij4: Difference between revisions
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{{Theoretical_model}} | |||
The | ==MODEL OF THE ALB2 I-DOMAIN / ICAM-1 D1 COMPLEX== | ||
<StructureSection load='1ij4' size='340' side='right'caption='[[1ij4]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJ4 FirstGlance]. <br> | |||
</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=1ij4 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1ij4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ij4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The interaction of the alphaLbeta2 integrin with its cellular ligand the intercellular adhesion molecule-1 (ICAM-1) is critical for the tight binding interaction between most leukocytes and the vascular endothelium before transendothelial migration to the sites of inflammation. In this article we have modeled the alphaL subunit I-domain in its active form, which was computationally docked with the D1 domain of the ICAM-1 to probe potential protein-protein interactions. The experimentally observed key interaction between the carboxylate of Glu 34 in the ICAM-1 D1 domain and the metal ion-dependent adhesion site (MIDAS) in the open alphaL I-domain was consistently reproduced by our calculations. The calculations reveal the nature of the alphaLbeta2/ICAM-1 interaction and suggest an explanation for the increased ligand-binding affinity in the "open" versus the "closed" conformation of the alphaL I-domain. A mechanism for substrate selectivity among alphaL, alphaM, and alpha2 I-domains is suggested whereby the orientation of the loops within the I-domain is critical in mediating the interaction of the Glu 34 carboxylate of ICAM-1 D1 with the MIDAS. | |||
Model of the alphaLbeta2 integrin I-domain/ICAM-1 DI interface suggests that subtle changes in loop orientation determine ligand specificity.,Legge GB, Morris GM, Sanner MF, Takada Y, Olson AJ, Grynszpan F Proteins. 2002 Aug 1;48(2):151-60. PMID:12112684<ref>PMID:12112684</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ij4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Grynszpan, F]] | |||
[[Category: Legge, G B]] | |||
[[Category: Morris, G M]] | |||
[[Category: Olson, A J]] | |||
[[Category: Sanner, M F]] | |||
[[Category: Takada, Y]] | |||
Latest revision as of 11:01, 4 August 2021
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MODEL OF THE ALB2 I-DOMAIN / ICAM-1 D1 COMPLEX
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