Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors Academic Article uri icon

Overview

MeSH Major

  • Factor X
  • Macrophage-1 Antigen
  • Viral Envelope Proteins

abstract

  • Three spatially distant surface loops were found to mediate the interaction of the coagulation protein factor X with the leukocyte integrin Mac-1. This interacting region, which by computational modeling defines a three-dimensional macromotif in the catalytic domain, was also recognized by glycoprotein C (gC), a factor X receptor expressed on herpes simplex virus (HSV)-infected endothelial cells. Peptidyl mimicry of each loop inhibited factor X binding to Mac-1 and gC, blocked monocyte generation of thrombin, and prevented monocyte adhesion to HSV-infected endothelium. These data link the ligand recognition of Mac-1 to established mechanisms of receptor-mediated vascular injury.

publication date

  • December 1991

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 1957171

Additional Document Info

start page

  • 1200

end page

  • 2

volume

  • 254

number

  • 5035