Open AccessX‐ray crystallographic characterization of rhesus macaque MHC Mamu‐A*02 complexed with an immunodominant SIV‐Gag nonapeptide
Author(s) -
Feng Youjun,
Qi Jianxun,
Zhang Huimin,
Wang Jinzi,
Liu Jinhua,
Jiang Fan,
Gao Feng
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105038704
Subject(s) - rhesus macaque , simian immunodeficiency virus , macaque , ctl* , mhc class i , virology , major histocompatibility complex , biology , cytotoxic t cell , transporter associated with antigen processing , virus , immunology , antigen , genetics , in vitro , neuroscience
Simian immunodeficiency virus (SIV) in the rhesus macaque is regarded as a classic animal model, playing a crucial role in HIV vaccine strategies and therapeutics by characterizing various cytotoxic T‐lymphocyte (CTL) responses in macaque monkeys. However, the availability of well documented structural reports focusing on rhesus macaque major histocompatibility complex class I (MHC I) molecules remains extremely limited. Here, a complex of the rhesus macaque MHC I molecule (Mamu‐A*02) with human β 2 m and an immunodominant SIV‐Gag nonapeptide, GESNLKSLY (GY9), has been crystallized. The crystal diffracts X‐rays to 2.7 Å resolution and belongs to space group C 2, with unit‐cell parameters a = 124.11, b = 110.45, c = 100.06 Å, and contains two molecules in the asymmetric unit. The availability of the structure, which is being solved by molecular replacement, will provide new insights into rhesus macaque MHC I (Mamu‐A*02) presenting pathogenic SIV peptides.