Open AccessComplex assembly, crystallization and preliminary X‐ray crystallographic studies of the swine major histocompatibility complex molecule SLA‐1*1502
Author(s) -
Pan Xiaocheng,
Qi Jianxun,
Zhang Nianzhi,
Li Qirun,
Yin Chunsheng,
Chen Rong,
Gao Feng,
Xia Chun
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911100741x
Subject(s) - porcine reproductive and respiratory syndrome virus , ctl* , epitope , major histocompatibility complex , crystallization , crystallography , molecule , mhc class i , ternary operation , chemistry , virus , biology , virology , immune system , cd8 , antigen , genetics , computer science , programming language , organic chemistry
In order to illustrate the structure of the swine MHC class I (SLA‐I) molecule and to evaluate the cytotoxic T lymphocyte (CTL) response against porcine reproductive and respiratory syndrome virus (PRRSV), the ternary complex of the SLA‐I molecule termed SLA‐1*1502 with β 2 ‐microglobulin and the CTL epitope TMPPGFELY (PRRSV‐NSP9 TY9 ) derived from PRRSV nonstructural protein 9 (residues 198–206) was assembled and crystallized. The crystal diffracted X‐rays to 2.2 Å resolution and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 66.1, b = 74.1, c = 98.6 Å; it contained one molecule in the asymmetric unit. The Matthews coefficient and the solvent content were calculated to be 2.74 Å 3 Da −1 and 55.17%, respectively. The results will be helpful in obtaining insight into the structural basis of the presentation of viral epitopes by SLA‐I.