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 A resolution and belonged to the sp. gr. C121, with the unit-cell parameters a = 206.46 A, b = 41.47 A, c = 106.74 A. The Matthews coefficient and solvent content were calculated to be 2.30 A3 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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