1t0p
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(New page: 200px<br /> <applet load="1t0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0p, resolution 1.66Å" /> '''Structural Basis of...)
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Revision as of 17:12, 12 November 2007
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Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A
Overview
Within the Ig superfamily (IgSF), intercellular adhesion molecules (ICAMs), form a subfamily that binds the leukocyte integrin alphaLbeta2. We report, a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1), in complex with the inserted domain, the ligand-binding domain of, alphaLbeta2. This high-resolution structure and comparisons among ICAM, subfamily members establish that the binding of ICAM-3 D1 onto the, inserted domain represents a common docking mode for ICAM subfamily, members. The markedly different off-rates of ICAM-1, -2, and -3 appear to, be determined by the hydrophobicity of residues that surround a metal, coordination bond in the alphaLbeta2-binding interfaces. Variation in, composition of glycans on the periphery of the interfaces influences, on-rate.
About this Structure
1T0P is a Protein complex structure of sequences from Homo sapiens with NAG and MG as ligands. Full crystallographic information is available from OCA.
Reference
An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2., Song G, Yang Y, Liu JH, Casasnovas JM, Shimaoka M, Springer TA, Wang JH, Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3366-71. Epub 2005 Feb 22. PMID:15728350
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