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1ij4

From Proteopedia

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'''Theoretical Model'''
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{{Theoretical_model}}
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The entry 1IJ4 is a Theoretical Model titled 'Model of the aLb2 I-domain / ICAM-1 D1 complex'.
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==MODEL OF THE ALB2 I-DOMAIN / ICAM-1 D1 COMPLEX==
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<StructureSection load='1ij4' size='340' side='right'caption='[[1ij4]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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[[Category:Theoretical Model]]
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 30 09:50:08 2008''
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</div>
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<div class="pdbe-citations 1ij4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Theoretical Model]]
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[[Category: Large Structures]]
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[[Category: Grynszpan, F]]
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[[Category: Legge, G B]]
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[[Category: Morris, G M]]
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[[Category: Olson, A J]]
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[[Category: Sanner, M F]]
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[[Category: Takada, Y]]

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL OF THE ALB2 I-DOMAIN / ICAM-1 D1 COMPLEX

PDB ID 1ij4

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