MODELING OF THE HUMAN INTERCELLULAR-ADHESION MOLECULE-1, THE HUMAN RHINOVIRUS MAJOR GROUP RECEPTOR

被引：55

作者：

GIRANDA, VL ^{[1
]}

CHAPMAN, MS ^{[1
]}

ROSSMANN, MG ^{[1
]}

机构：

[1] PURDUE UNIV,DEPT BIOL SCI,W LAFAYETTE,IN 47907

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1990年 / 7卷 / 03期

关键词：

docking receptor to virus; ICAM‐1; immunoglobulin superfamily; rhinovirus receptor; structure prediction;

D O I：

10.1002/prot.340070304

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A model has been built of the amino‐terminal domain of the intercellular adhesion molecule‐1 (ICAM‐1), the receptor for most human rhinovirus serotypes. The model was based on sequence and presumed structural homology to immunoglobulin constant domains. It fits well into the putative receptors attachment site, the canyon, on the human rhinovirus‐14 (HRV14) surface in a manner consistent with most of the mutational data for ICMA‐1 (Staunton, D. E., Dustin, M. L., Erickson, H. P., Springer, T. A. Cell, in press, 1989) and HRV14 (Colonno, R. J., Condra, J. H., Mizutani, S., Callahan, P. L., Davies, M. E., Murcko, M. A. Proc. Natl. Acad. Sci. U.S.A. 85: 5449‐5453, 1988). Copyright © 1990 Wiley‐Liss, Inc.

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页码：227 / 233

页数：7

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