1iam

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spinqualitylabelsall models 1iam, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The normal function of human intercellular adhesion molecule-1 (ICAM-1) is, to provide adhesion between endothelial cells and leukocytes after injury, or stress. ICAM-1 binds to leukocyte function-associated antigen (LFA-1), or macrophage-1 antigen (Mac-1). However, ICAM-1 is also used as a, receptor by the major group of human rhinoviruses and is a catalyst for, the subsequent viral uncoating during cell entry. The three-dimensional, atomic structure of the two amino-terminal domains (D1 and D2) of ICAM-1, has been determined to 2.2-A resolution and fitted into a cryoelectron, microscopy reconstruction of a rhinovirus-ICAM-1 complex. Rhinovirus, attachment is confined to the BC, CD, DE, and FG loops of the, amino-terminal Ig-like domain (D1) at the end distal to the cellular, membrane. The loops are considerably different in structure to those of, human ICAM-2 or murine ICAM-1, which do not bind rhinoviruses. There are, extensive charge interactions between ICAM-1 and human rhinoviruses, which, are mostly conserved in both major and minor receptor groups of, rhinoviruses. The interaction of ICAMs with LFA-1 is known to be mediated, by a divalent cation bound to the insertion (I)-domain on the alpha chain, of LFA-1 and the carboxyl group of a conserved glutamic acid residue on, ICAMs. Domain D1 has been docked with the known structure of the I-domain., The resultant model is consistent with mutational data and provides a, structural framework for the adhesion between these molecules.

Disease

Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[147840]

About this Structure

1IAM is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Full crystallographic information is available from OCA.

Reference

The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand., Bella J, Kolatkar PR, Marlor CW, Greve JM, Rossmann MG, Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4140-5. PMID:9539703

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