4.0 Article

Complex assembly, crystallization and preliminary X-ray crystallographic studies of the swine major histocompatibility complex molecule SLA-1*1502

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S174430911100741X

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Funding

  1. Ministry of Science and Technology of China [2009ZX08009-150B]
  2. National Key Basic Research Program of China (973 Program) [2007CB815805]

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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 beta(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 angstrom resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 66.1, b = 74.1, c = 98.6 angstrom; it contained one molecule in the asymmetric unit. The Matthews coefficient and the solvent content were calculated to be 2.74 angstrom(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.

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