Zhou, Minghai, Xu, Yanhui, Lou, Zhiyong, Cole, David ![]() |
Abstract
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 β2m 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 P2221, with unit-cell parameters a = 89.082, b = 110.398, c = 47.015 Å, α = β = γ = 90°. The crystals contain one complex per asymmetric unit and diffract X-rays to at least 2.06 Å resolution. The structure has been solved by molecular replacement and is the first crystal structure of a peptide–H-2Kd complex.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Medicine Systems Immunity Research Institute (SIURI) |
Subjects: | R Medicine > R Medicine (General) |
Uncontrolled Keywords: | murine class I major histocompatibility antigen complex; hepatitis B virus-core nonapeptide |
Publisher: | International Union of Crystallography |
ISSN: | 0907-4449 |
Last Modified: | 25 Oct 2022 09:56 |
URI: | https://orca.cardiff.ac.uk/id/eprint/60525 |
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