Purification, crystallization and preliminary X-ray diffraction analysis of the human major histocompatibility antigen HLA-B*2703 complexed with a viral peptide and with a self-peptide

人主要组织相容性抗原HLA-B*2703与病毒肽和自身肽复合物的纯化、结晶和初步X射线衍射分析

阅读:1

Abstract

The product of the human leukocyte antigen (HLA) gene HLA-B*2703 differs from that of the prototypical subtype HLA-B*2705 by a single amino acid at heavy-chain residue 59 that is involved in anchoring the peptide N-terminus within the A pocket of the molecule. Two B*2703-peptide complexes were crystallized using the hanging-drop vapour-diffusion method using PEG 8000 as a precipitant. The crystals belong to space group P2(1) (pVIPR peptide) or P2(1)2(1)2(1) (pLMP2 peptide). Data sets were collected to 1.55 A (B*2703-pVIPR) or 2.0 A (B*2703-pLMP2) resolution using synchrotron radiation. With B*2705-pVIPR as a search model, a clear molecular-replacement solution was found for both B*2703 complexes.

特别声明

1、本页面内容包含部分的内容是基于公开信息的合理引用;引用内容仅为补充信息,不代表本站立场。

2、若认为本页面引用内容涉及侵权,请及时与本站联系,我们将第一时间处理。

3、其他媒体/个人如需使用本页面原创内容,需注明“来源:[生知库]”并获得授权;使用引用内容的,需自行联系原作者获得许可。

4、投稿及合作请联系:info@biocloudy.com。