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由内质网后抗原结合所决定的MHC II类分子结构、占据情况及表面表达

MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding.

作者信息

Germain R N, Hendrix L R

机构信息

Lymphocyte Biology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.

出版信息

Nature. 1991 Sep 12;353(6340):134-9. doi: 10.1038/353134a0.

Abstract

Class II major histocompatibility complex molecules undergo a change in structure upon stable binding of peptide antigen. Analysis of the site and extent of this change among class II molecules of splenic antigen-presenting cells reveals the preference of class II for peptide acquisition outside the endoplasmic reticulum and indicates that the class II presentation system is not saturated with self peptides. There are numerous empty class II molecules on the cell surface and peptide antigen is evidently important in regulating surface class II expression.

摘要

II类主要组织相容性复合体分子在与肽抗原稳定结合后会发生结构变化。对脾抗原呈递细胞的II类分子中这种变化的位点和程度进行分析,揭示了II类分子在内质网外获取肽的偏好,并表明II类呈递系统未被自身肽饱和。细胞表面存在大量空的II类分子,肽抗原显然在调节表面II类分子表达中起重要作用。

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