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HLA - B27的结构显示出以延伸构象结合的九聚体自身肽。

The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation.

作者信息

Madden D R, Gorga J C, Strominger J L, Wiley D C

机构信息

Committee on Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts.

出版信息

Nature. 1991 Sep 26;353(6342):321-5. doi: 10.1038/353321a0.

DOI:10.1038/353321a0
PMID:1922337
Abstract

X-ray crystallography reveals electron density in the antigen-binding site of HLA-B27 that is an interpretable image of nonameric peptides in a largely extended conformation. Clear density exists for the main chain and several side chains and is consistent with the sequence of 11 nonameric self-peptides eluted from HLA-B27. Pockets in the antigen-binding cleft bind four side chains and the amino and carboxyl termini of the peptide.

摘要

X射线晶体学揭示了HLA - B27抗原结合位点的电子密度,这是处于大致伸展构象的九聚体肽的可解释图像。主链和几个侧链存在清晰的密度,并且与从HLA - B27洗脱的11种九聚体自身肽的序列一致。抗原结合裂隙中的口袋结合肽的四个侧链以及氨基和羧基末端。

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