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

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 Å{sup 3} Da{sup –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.

Authors:
; ;  [1]
  1. Zhoukou Normal University, College of Life Science and Agronomy (China)
Publication Date:
OSTI Identifier:
22758236
Resource Type:
Journal Article
Journal Name:
Crystallography Reports
Additional Journal Information:
Journal Volume: 63; Journal Issue: 3; Other Information: Copyright (c) 2018 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1063-7745
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 60 APPLIED LIFE SCIENCES; CHINA; CRYSTALLOGRAPHY; CRYSTALS; GENES; HEMAGGLUTININS; HISTOCOMPATIBILITY COMPLEX; INFLUENZA; LEUKOCYTES; MOLECULES; PEPTIDES; RESOLUTION; SWINE; VIRUSES; X RADIATION

Citation Formats

Fan, Shuhua, Wang, Yongli, and Wang, Xian. X-ray Crystallographic Characterization of the Swine MHC I Molecule SLA-3*0202 Complexed with IAV-HA Nonapeptide. United States: N. p., 2018. Web. doi:10.1134/S106377451803032X.
Fan, Shuhua, Wang, Yongli, & Wang, Xian. X-ray Crystallographic Characterization of the Swine MHC I Molecule SLA-3*0202 Complexed with IAV-HA Nonapeptide. United States. doi:10.1134/S106377451803032X.
Fan, Shuhua, Wang, Yongli, and Wang, Xian. Tue . "X-ray Crystallographic Characterization of the Swine MHC I Molecule SLA-3*0202 Complexed with IAV-HA Nonapeptide". United States. doi:10.1134/S106377451803032X.
@article{osti_22758236,
title = {X-ray Crystallographic Characterization of the Swine MHC I Molecule SLA-3*0202 Complexed with IAV-HA Nonapeptide},
author = {Fan, Shuhua and Wang, Yongli and Wang, Xian},
abstractNote = {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 Å{sup 3} Da{sup –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.},
doi = {10.1134/S106377451803032X},
journal = {Crystallography Reports},
issn = {1063-7745},
number = 3,
volume = 63,
place = {United States},
year = {2018},
month = {5}
}