Article
Structure-function analysis of Yersinia pestis YopM's interaction with alpha-thrombin to rule on its significance in systemic plague and to model YopM's mechanism of binding host proteins.
Microbial pathogenesis - 1 Apr 2001
Hines J, Skrzypek E, Kajava A V, Straley S C
Abstract excerpt
The plague virulence protein YopM of Yersinia pestis KIM5 belongs to the large family of leucine-rich repeat (LRR) proteins. The only activity demonstrated so far for YopM is thrombin-binding, which could be a function of the small amount of YopM that is released into surrounding tissues by the bacteria. This study combined deletional and mutational analysis, chemical crosslinking assays, and in vitro functional...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.