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Ab Initio Prediction of Peptide-MHC Binding Geometry for Diverse Class I MHC Allotypes
 

Summary: Ab Initio Prediction of Peptide-MHC Binding Geometry for
Diverse Class I MHC Allotypes
Andrew J. Bordner1,2* and Ruben Abagyan1
1
Department of Molecular Biology, The Scripps Research Institute, San Diego, California
2
Computer Science and Mathematics Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee
ABSTRACT Since determining the crystallo-
graphic structure of all peptide-MHC complexes is
infeasible, an accurate prediction of the conforma-
tion is a critical computational problem. These mod-
els can be useful for determining binding energet-
ics, predicting the structures of specific ternary
complexes with T-cell receptors, and designing new
molecules interacting with these complexes. The
main difficulties are (1) adequate sampling of the
large number of conformational degrees of freedom
for the flexible peptide, (2) predicting subtle changes
in the MHC interface geometry upon binding, and
(3) building models for numerous MHC allotypes

  

Source: Abagyan, Ruben - School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego

 

Collections: Biology and Medicine