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Updated: May 14, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Complex assembly, crystallization and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule
Beibei Sun1, Xiaoying Li, Zhenbao Wang
1Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing 100193, People's Republic of China.
Abstract:
The chicken major histocompatibility complex (MHC) class I molecules named BF are strongly associated with Marek's disease (MD). A single structure, that of chicken BF2*2101 from the B21 haplotype, which might provide resistance to MD, has been determined. However, little is known about other structures apart from BF2*2101. In order to provide further structures of chicken MHC class I molecules, BF2*1501 and chicken β(2)-microglobulin complexed with a nonapeptide (MDV-MEQ(RRR9)) derived from Marek's disease virus MEQ protein (MDV EcoRI Q fragment, residues 72-80) were assembled and crystallized. Diffraction data from the crystal were collected to 2.6 Å resolution; the crystal belonged to space group P3(1)21, with unit-cell parameters a = 125.1, b = 125.1, c = 80.9 Å and two molecules in the asymmetric unit. The Matthews coefficient V(M) was 2.08 Å(3) Da(-1), with a calculated solvent content of 40.78%. These data will be helpful in obtaining insight into the structural basis of the involvement of BF2*1501 in MD.
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