Dynamic influence of the two membrane-proximal immunoglobulin-like domains upon the peptide-binding platform domain in class I and class II major histocompatibility complexes: normal mode analysis.
作者： Hiroyuki Nojima , Kazuhiko Kanou , Kenshu Kamiya , Koichiro Atsuda , Hideaki Umeyama
DOI: 10.1248/CPB.57.1193
关键词:
摘要: Major histocompatibility complexes (MHCs) mainly fall into class I and II. The two classes have similar structures, with membrane-proximal immunoglobulin-like domains a peptide-binding platform domain, though their organizations are different. We simulated the dynamics of whole partial model deficient in either for II using normal mode analysis. Our study showed that influence upon domain were decisively different between I. Both (the α2 β2 domains) MHC, especially influenced most important pocket accommodates large hydrophobic anchor side chain N-terminal bound peptide, was not neighborhood. By contrast, α3 β2m MHC had little residue peptide. These results suggest greater than those MHC.
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