1IAM

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

Summary for 1IAM

• Entry DOI: 10.2210/pdb1iam/pdb
• Descriptor: INTERCELLULAR ADHESION MOLECULE-1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: rhinovirus receptor, cell adhesion, integrin ligand, glycoprotein, lfa-1 ligand, immunoglobulin fold, transmembrane, viral protein receptor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 20701.55

Authors

Bella, J.,Kolatkar, P.R.,Marlor, C.,Greve, J.M.,Rossmann, M.G. (deposition date: 1998-02-22, release date: 1998-04-29, Last modification date: 2024-10-30)

Primary citation

Bella, J.,Kolatkar, P.R.,Marlor, C.W.,Greve, J.M.,Rossmann, M.G.
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.
Proc.Natl.Acad.Sci.USA, 95:4140-4145, 1998

PubMed Abstract: 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.

PubMed: 9539703
DOI: 10.1073/pnas.95.8.4140

Experimental method

X-RAY DIFFRACTION (2.1 Å)