Please use this identifier to cite or link to this item: https://doi.org/10.1073/pnas.95.8.4140
Title: 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
Authors: Bella, J.
Kolatkar, P.R. 
Marlor, C.W.
Greve, J.M.
Rossmann, M.G.
Issue Date: 14-Apr-1998
Citation: Bella, J., Kolatkar, P.R., Marlor, C.W., Greve, J.M., Rossmann, M.G. (1998-04-14). 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. Proceedings of the National Academy of Sciences of the United States of America 95 (8) : 4140-4145. ScholarBank@NUS Repository. https://doi.org/10.1073/pnas.95.8.4140
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-Å 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 domains (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 a chain of LFA, I 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.
Source Title: Proceedings of the National Academy of Sciences of the United States of America
URI: http://scholarbank.nus.edu.sg/handle/10635/113190
ISSN: 00278424
DOI: 10.1073/pnas.95.8.4140
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