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X-ray Crystallographic Characterization of the Swine MHC I Molecule SLA-3*0202 Complexed with IAV-HA Nonapeptide

  • Structure of Macromolecular Compounds
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Abstract

The swine major histocompatibility complex (MHC) class I molecules are also called swine leukocyte antigen (SLA), and most of the highly polymorphic SLA genes are associated with swine diseases. However, the well documented structural reports on swine MHC I molecules remain quite limited. In order to clarify the structural characteristics of the Chinese heishan wild boar MHC class I molecule, SLA-3*0202 and swine β2-microglobulin (sβ2m) with a KMNTQFTAV nonapeptide derived from Influenza A virus Hemagglutinin protein (IAV-HA) were assembled and crystallized. The crystal diffracted at 1.55 Å resolution and belonged to the sp. gr. C121, with the unit-cell parameters a = 206.46 Å, b = 41.47 Å, c = 106.74 Å. The Matthews coefficient and solvent content were calculated to be 2.30 Å3 Da–1 and 46.64%, respectively. The availability of the structure, which is being solved by molecular replacement, will provide new insights into swine MHC I presenting IAV peptides.

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Authors and Affiliations

  1. College of Life Science and Agronomy, Zhoukou Normal University, Zhoukou, 466001, P. R. China

    Shuhua Fan, Yongli Wang & Xian Wang

Authors
  1. Shuhua Fan
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  2. Yongli Wang
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  3. Xian Wang
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Correspondence to Shuhua Fan.

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Fan, S., Wang, Y. & Wang, X. X-ray Crystallographic Characterization of the Swine MHC I Molecule SLA-3*0202 Complexed with IAV-HA Nonapeptide. Crystallogr. Rep. 63, 428–432 (2018). https://doi.org/10.1134/S106377451803032X

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  • DOI: https://doi.org/10.1134/S106377451803032X

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