1ic1
From Proteopedia
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THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1
Contents |
Overview
The 3.0-A structure of a 190-residue fragment of intercellular adhesion, molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF), domains. Each of two independent molecules dimerizes identically with a, symmetry-related molecule over a hydrophobic interface on the BED sheet of, domain 1, in agreement with dimerization of ICAM-1 on the cell surface., The residues that bind to the integrin LFA-1 are well oriented for, bivalent binding in the dimer, with the critical Glu-34 residues pointing, away from each other on the periphery. Residues that bind to rhinovirus, are in the flexible BC and FG loops at the tip of domain 1, and these and, the upper half of domain 1 are well exposed in the dimer for docking to, virus. By contrast, a residue important for binding to Plasmodium, falciparum-infected erythrocytes is in the dimer interface. The presence, of A' strands in both domains 1 and 2, conserved hydrogen bonds at domain, junctions, and elaborate hydrogen bond networks around the key integrin, binding residues in domain 1 make these domains suited to resist tensile, forces during adhesive interactions. A subdivision of the intermediate (I), set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously, described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
Disease
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[147840]
About this Structure
1IC1 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1., Casasnovas JM, Stehle T, Liu JH, Wang JH, Springer TA, Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4134-9. PMID:9539702
Page seeded by OCA on Fri Feb 15 16:00:43 2008
