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基于肽侧链扫描的主要组织相容性复合体II类-肽相互作用的精确预测。

Precise prediction of major histocompatibility complex class II-peptide interaction based on peptide side chain scanning.

作者信息

Hammer J, Bono E, Gallazzi F, Belunis C, Nagy Z, Sinigaglia F

机构信息

Roche Milano Ricerche, Milan, Italy.

出版信息

J Exp Med. 1994 Dec 1;180(6):2353-8. doi: 10.1084/jem.180.6.2353.

DOI:10.1084/jem.180.6.2353
PMID:7964508
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2191799/
Abstract

We describe here a new method for predicting class II major histocompatibility complex-binding peptides, based on the preferences observed in a systematic series of peptide binding experiments where each position in a "minimal" peptide was replaced individually by every amino acid. The DRB1*0401 peptide binding preferences were determined and incorporated into a computer program that looks through sequences for potential epitopes and assigns each a score. These scores correlate well with previously determined T cell epitopes of foreign antigens and endogenous peptides from self proteins. Our findings hold implications for the design of subunit vaccines and in the identification of autoantigenic peptide regions within self proteins.

摘要

我们在此描述一种预测II类主要组织相容性复合体结合肽的新方法,该方法基于在一系列系统的肽结合实验中观察到的偏好,在这些实验中,一个“最小”肽中的每个位置被逐个氨基酸替换。确定了DRB1*0401肽的结合偏好,并将其纳入一个计算机程序,该程序在序列中寻找潜在的表位并为每个表位赋予一个分数。这些分数与先前确定的外来抗原和自身蛋白质内源性肽的T细胞表位密切相关。我们的发现对亚单位疫苗的设计以及自身蛋白质内自身抗原肽区域的鉴定具有启示意义。

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Promiscuous and allele-specific anchors in HLA-DR-binding peptides.HLA-DR结合肽中的混杂性和等位基因特异性锚定残基
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High-affinity binding of short peptides to major histocompatibility complex class II molecules by anchor combinations.通过锚定组合实现短肽与主要组织相容性复合体II类分子的高亲和力结合。
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