Complex assembly, crystallization and preliminary X-ray crystallographic studies of the swine major histocompatibility complex molecule SLA-11502

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 β2‐microglobulin and the CTL...

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Veröffentlicht in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-05, Vol.67 (5), p.568-571
Hauptverfasser: Pan, Xiaocheng, Qi, Jianxun, Zhang, Nianzhi, Li, Qirun, Yin, Chunsheng, Chen, Rong, Gao, Feng, Xia, Chun
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Sprache:eng
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Zusammenfassung: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 β2‐microglobulin and the CTL epitope TMPPGFELY (PRRSV‐NSP9TY9) 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 P212121, 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 Å3 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.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S174430911100741X