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 |
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Format: | Artikel |
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. |
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ISSN: | 1744-3091 1744-3091 2053-230X |
DOI: | 10.1107/S174430911100741X |