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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors.

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.[1]

References

  1. Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors. Altieri, D.C., Etingin, O.R., Fair, D.S., Brunck, T.K., Geltosky, J.E., Hajjar, D.P., Edgington, T.S. Science (1991) [Pubmed]
 
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