Complex assembly, crystallization and preliminary X‐ray crystallographic analysis of the chicken MHC class I molecule BF2*1501. Issue 2 (5th February 2013)

• Record Type: Journal Article
• Authors: Sun, Beibei; Li, Xiaoying; Wang, Zhenbao; Xia, Chun
• Is Part Of: Acta crystallographica. Volume 69:Issue 2(2013:Feb.)
• Page Start: 122
• Page End: 125
• Publication Date: 2013-02-05
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309112050300
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 β₂‐microglobulin complexed with a nonapeptide (MDV‐MEQ_RRR9) derived from Marek's disease virus MEQ protein (MDV <italic>Eco</italic>RI 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 <italic>P</italic>3₁21, with unit‐cell parameters <italic>a</italic> = 125.1, <italic>b</italic> = 125.1, <italic>c</italic> = 80.9 Å and two molecules in the asymmetric unit. The Matthews coefficient <italic>V</italic>_M was 2.08 ų 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.</p> </abstract>