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Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif

Academic Article
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Overview

authors

  • Zhu, Y. R.
  • Rudensky, A. Y.
  • Corper, A. L.
  • Teyton, Luc
  • Wilson, Ian

publication date

  • February 2003

journal

  • Journal of Molecular Biology  Journal

abstract

  • Association between the class II major histocompatibility complex (MHC) and the class II invariant chain-associated peptide (CLIP) occurs naturally as an intermediate step in the MHC class II processing pathway. Here, we report the crystal structure of the murine class II MHC molecule I-A(b) in complex with human CLIP at 2.15A resolution. The structure of I-A(b) accounts, via the peptide-binding groove's unique physicochemistry, for the distinct peptide repertoire bound by this allele. CLIP adopts a similar conformation to peptides bound by other I-A alleles, reinforcing the notion that CLIP is presented as a conventional peptide antigen. When compared to the related HLA-DR3/CLIP complex structure, the CLIP peptide displays a slightly different conformation and distinct interaction pattern with residues in I-A(b). In addition, after examining the published sequences of peptides presented by I-A(b), we discuss the possibility of predicting peptide alignment in the I-A(b) binding groove using a simple scoring matrix.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antigens, Differentiation, B-Lymphocyte
  • Binding Sites
  • Crystallography, X-Ray
  • Genes, MHC Class II
  • Histocompatibility Antigens Class II
  • Humans
  • Hydrogen Bonding
  • Macromolecular Substances
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Sequence Alignment
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Research

keywords

  • MHC class II
  • antigen presentation
  • invariant chain
  • peptide binding
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/s0022-2836(02)01437-7

PubMed ID

  • 12589760
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Additional Document Info

start page

  • 1157

end page

  • 1174

volume

  • 326

issue

  • 4

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