Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add filters








Language
Year range
1.
J Biosci ; 2003 Apr; 28(3): 265-71
Article in English | IMSEAR | ID: sea-110900

ABSTRACT

Vaccinia virus complement control protein (VCP) was one of the first viral molecules demonstrated to have a role in blocking complement and hence in the evasion of host defense. Structurally it is very similar to the human C4b-BP and the other members of complement control protein. Functionally it is most similar to the CR1 protein. VCP blocks both major pathways of complement activation. The crystal structure of VCP was determined a little over a year ago and it is the only known structure of an intact and complete complement control protein. In addition to binding complement, VCP also binds to heparin. These two binding abilities can take place simultaneously and contribute to its many function and to its potential use in several inflammatory diseases, e.g. Alzheimer's disease (AD), CNS injury, xenotransplantation, etc. making it a truly fascinating molecule and potential drug.


Subject(s)
Complement Activation , Complement Inactivator Proteins/chemistry , Complement System Proteins/physiology , Heparin/metabolism , Humans , Immune System/physiology , Protein Binding , Receptors, Complement 3b/metabolism , Vaccinia virus/metabolism , Viral Proteins/chemistry
SELECTION OF CITATIONS
SEARCH DETAIL