Dynamic influence of the two membrane-proximal immunoglobulin-like domains upon the peptide-binding platform domain in class 1 and class 2 major histocompatibility complexes: normal mode analysis

DOI Web Site Web Site 被引用文献2件 参考文献39件

書誌事項

タイトル別名
  • 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

この論文をさがす

抄録

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

収録刊行物

被引用文献 (2)*注記

もっと見る

参考文献 (39)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ