Open AccessComplex assembly, crystallization and preliminary X‐ray crystallographic studies of rhesus macaque MHC Mamu‐A*01 complexed with an immunodominant SIV‐Gag nonapeptide
Author(s) -
Chu Fuliang,
Lou Zhiyong,
Gao Bin,
Bell John I.,
Rao Zihe,
Gao George F.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105016453
Subject(s) - simian immunodeficiency virus , rhesus macaque , ctl* , macaque , virology , major histocompatibility complex , biology , mhc class i , cytotoxic t cell , virus , epitope , transporter associated with antigen processing , peptide , antigen , in vitro , immunology , genetics , biochemistry , paleontology
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 β 2 m 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 I 422, with unit‐cell parameters a = b = 183.8, c = 155.2 Å. The crystal contains two molecules in the asymmetric unit and diffracts X‐rays to 2.8 Å 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