Please use this identifier to cite or link to this item:
https://doi.org/10.1073/pnas.95.8.4140
DC Field | Value | |
---|---|---|
dc.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 | |
dc.contributor.author | Bella, J. | |
dc.contributor.author | Kolatkar, P.R. | |
dc.contributor.author | Marlor, C.W. | |
dc.contributor.author | Greve, J.M. | |
dc.contributor.author | Rossmann, M.G. | |
dc.date.accessioned | 2014-11-30T06:40:49Z | |
dc.date.available | 2014-11-30T06:40:49Z | |
dc.date.issued | 1998-04-14 | |
dc.identifier.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 | |
dc.identifier.issn | 00278424 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/113190 | |
dc.description.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. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1073/pnas.95.8.4140 | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | BIOINFORMATICS CENTRE | |
dc.description.doi | 10.1073/pnas.95.8.4140 | |
dc.description.sourcetitle | Proceedings of the National Academy of Sciences of the United States of America | |
dc.description.volume | 95 | |
dc.description.issue | 8 | |
dc.description.page | 4140-4145 | |
dc.description.coden | PNASA | |
dc.identifier.isiut | 000073120800015 | |
Appears in Collections: | Staff Publications |
Show simple item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.