A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1

• DOI: 10.1073/pnas.95.8.4134
• Publication Date: 2002-07-26T14:40:11Z
• Authors: José M. Casasnovas; Thilo Stehle; Jin-huan Liu; Jia-huai Wang; Timothy A. Springer
• Keywords: Immunoglobulin superfamily; Docking (animal)

The 3.0-A structure of a 190-residue fragment intercellular adhesion molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF) domains. Each independent molecules dimerizes identically with symmetry-related molecule over hydrophobic interface on the BED sheet domain 1, in agreement dimerization ICAM-1 cell surface. residues that bind to integrin LFA-1 are well oriented for bivalent binding dimer, critical Glu-34 pointing away from each other periphery. Residues rhinovirus flexible BC and FG loops at tip these upper half 1 exposed dimer docking virus. By contrast, residue important Plasmodium falciparum-infected erythrocytes is interface. presence A' strands both domains 2, conserved hydrogen bonds junctions, elaborate bond networks around key make suited resist tensile forces during adhesive interactions. A subdivision intermediate (I) set IgSF proposed which previously described I belong I1 2 ICAM-1, ICAM-2, vascular I2 set.