X-ray crystallographic characterization of rhesus macaque MHC Mamu-A*02 complexed with an immunodominant SIV-Gag nonapeptide

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Youjun FengFeng Gao

Abstract

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 beta2m and an immunodominant SIV-Gag nonapeptide, GESNLKSLY (GY9), has been crystallized. The crystal diffracts X-rays to 2.7 A resolution and belongs to space group C2, with unit-cell parameters a = 124.11, b = 110.45, c = 100.06 A, 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.

References

Apr 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·D N GarbocziD C Wiley
Jan 1, 1990·Annals of the New York Academy of Sciences·H M McClureR F Schinazi
Jul 24, 2004·Acta Crystallographica. Section D, Biological Crystallography·Minghai ZhouGeorge F Gao
Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Fuliang ChuGeorge F Gao

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