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Simian immunodeficiency virus (SIV) infection in rhesus macaques has been used as the best model for the study of human immunodeficiency virus (HIV) infection in humans, especially in the cytotoxic T-lymphocyte (CTL) response. However, the structure of rhesus macaque (or any other monkey model) major histocompatibility complex class I (MHC I) presenting a specific peptide (the ligand for CTL) has not yet been elucidated. Here, using in vitro refolding, the preparation of the complex of the rhesus macaque MHC I allele (Mamu-A*01) with human beta2m and an immunodominant peptide, CTPYDINQM (Gag_CM9), derived from SIV Gag protein is reported. The complex (45 kDa) was crystallized; the crystal belongs to space group I422, with unit-cell parameters a = b = 183.8, c = 155.2 A. The crystal contains two molecules in the asymmetric unit and diffracts X-rays to 2.8 A resolution. The structure is being solved by molecular replacement and this is the first attempt to determined the crystal structure of a peptide-nonhuman primate MHC complex.

Original publication

DOI

10.1107/S1744309105016453

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/06/2005

Volume

61

Pages

614 - 616

Keywords

Amino Acid Sequence, Animals, Antigens, Viral, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Gene Products, gag, Histocompatibility Antigens Class I, Immunodominant Epitopes, Inclusion Bodies, Macaca mulatta, Peptide Fragments, Protein Binding, Simian Immunodeficiency Virus, Volatilization