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1dlh

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1dlh, resolution 2.80Å ()
Sites: , , , , , , and
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE

Publication Abstract from PubMed

An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.

Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide., Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC, Nature. 1994 Mar 17;368(6468):215-21. PMID:8145819

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1DLH is a 6 chains structure with sequences from Homo sapiens. The February 2005 RCSB PDB Molecule of the Month feature on Major Histocompatibility Complex by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_2. Full crystallographic information is available from OCA.

Reference

  • Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature. 1994 Mar 17;368(6468):215-21. PMID:8145819 doi:10.1038/368215a0

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