PMID: 9539703May 16, 1998Paper

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
J BellaM G Rossmann

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 c...Continue Reading

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Citations

Feb 13, 2001·Biochemical and Biophysical Research Communications·A K BeheraS S Mohapatra
Dec 22, 1999·Journal of Structural Biology·J Bella, M G Rossmann
Apr 2, 2003·Journal of Immunological Methods·Guang X LuoFang Fang
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Jul 31, 2013·Quarterly Reviews of Biophysics·Michael G Rossmann
Mar 5, 2009·Proceedings of the National Academy of Sciences of the United States of America·Sheng LiJianping Ding
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