Accuracy of a structural homology model for a class ii

Jeffrey L. Nauss, Scheherazade Sadegh-Nasseri

Research output: Contribution to journalArticlepeer-review

Abstract

Structural homology modeling is used to test the accuracy by which a Class I major histocompatibility complex (MHC) could be used to model a Class II MHC. The crystal structure of HLA-aw68 served as a reference molecule to model HLA-DR1. The resulting model was compared to the recently released crystal structure by Brown et al. (Nature, Vol. 364, p. 33-39 (1993)). The overall tertiary structure motif (two a-helices and a ß-sheet forming a peptide binding cleft) was maintained. However, significant deviations in the secondary structure elements were found between the model and the DR1 crystal structure. These deviations were consistent with the differences between Class I and Class II crystal structures. In regions where the model and DR1 crystal structures are most similar, side chain orientations are also similar. Specific peptide-MHC interactions are discussed and compared with the crystal structure results.

Original languageEnglish (US)
Pages (from-to)1213-1233
Number of pages21
JournalJournal of Biomolecular Structure and Dynamics
Volume12
Issue number6
DOIs
StatePublished - Jun 1995
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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