Complex assembly, crystallization and preliminary X-ray crystallographic studies of MHC H-2Kd complexed with an HBV-core nonapeptide.
In order to establish a system for structural studies of the murine class I major histocompatibility antigen complex (MHC) H-2Kd, a bacterial expression system and in vitro refolding preparation of the complex of H-2Kd with human beta2m and the immunodominant peptide SYVNTNMGL from hepatitis B virus (HBV) core-protein residues 87-95 was employed. The complex (45 kDa) was crystallized; the crystals belong to space group P222(1), with unit-cell parameters a = 89.082, b = 110.398, c = 47.015 A, alpha = beta = gamma = 90 degrees. The crystals contain one complex per asymmetric unit and diffract X-rays to at least 2.06 A resolution. The structure has been solved by molecular replacement and is the first crystal structure of a peptide-H-2Kd complex.
Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.
Minghai
M
Zhou
Yanhui
Y
Xu
Zhiyong
Z
Lou
David K
DK
Cole
Xiaojuan
X
Li
Yiwei
Y
Liu
Po
P
Tien
Zihe
Z
Rao
George F
GF
Gao
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D018360:Crystallography, X-Ray; D006183:H-2 Antigens / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D006515:Hepatitis B virus / Q000737:chemistry* / Q000276:immunology; D006801:Humans; D051379:Mice; D010446:Peptide Fragments / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D014758:Viral Core Proteins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D001613:beta 2-Microglobulin / Q000378:metabolism
D006183:H-2 Antigens; D010446:Peptide Fragments; D014758:Viral Core Proteins; D001613:beta 2-Microglobulin