1ij4: Difference between revisions

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~~{{Theoretical_model}}~~

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

== Structural highlights ==

<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IJ4 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ij4 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1ij4 PDBsum]</span></td></tr>

<table>

== 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.

~~[[Image~~:~~1ij4~~.~~png|left|200px]]~~

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>

~~{{STRUCTURE_1ij4| PDB=1ij4 | SCENE= }}~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

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

== References ==

~~{{ABSTRACT_PUBMED_12112684}}~~

__TOC__

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:012112684<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Grynszpan, F]]

[[Category: Legge, G B]]

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@@ Line 1: / Line 1: @@
-{{Theoretical_model}}
+==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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IJ4 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ij4 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1ij4 PDBsum]</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.
-[[Image:1ij4.png|left|200px]]
+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>
-{{STRUCTURE_1ij4|  PDB=1ij4  |  SCENE=  }}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-===MODEL OF THE ALB2 I-DOMAIN / ICAM-1 D1 COMPLEX===
+== References ==
+<references/>
-{{ABSTRACT_PUBMED_12112684}}
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:012112684</ref><references group="xtra"/>
 [[Category: Grynszpan, F]]
 [[Category: Legge, G B]]