O'Sullivan D, Sidney J, Del Guercio M F, Colón S M, Sette A
Cytel, La Jolla, CA 92037.
J Immunol. 1991 Feb 15;146(4):1240-6.
Peptide regions crucial for binding to four different DR alleles (DR1, DR2, DR5, and DR52a) have been localized in five unrelated DR binding peptides (dynorphin 1-13, sperm whale myoglobin 132-153, influenza hemagglutinin 307-319, pigeon cytochrome c 88-104, and tetanus toxoid 830-843) by testing panels of truncated analogs for DR binding. It was found that in most cases, different DR alleles recognize almost identical, albeit distinct, core regions, suggesting that different DR alleles may recognize similar structures on their peptide ligands. Furthermore, it was found that these core regions, notwithstanding their derivation from unrelated sequences, share a common structural pattern. When the sequences of several other unrelated determinants were scrutinized, the structural motif identified was present in some, but absent in other good DR binders, suggesting that good DR binding capacity of peptide molecules may be compatible with more than one single sequence pattern.
通过检测一系列截短类似物与DR的结合情况，已在5种不相关的DR结合肽（强啡肽1 - 13、抹香鲸肌红蛋白132 - 153、流感血凝素307 - 319、鸽细胞色素c 88 - 104和破伤风类毒素830 - 843）中定位了与4种不同DR等位基因（DR1、DR2、DR5和DR52a）结合至关重要的肽段区域。研究发现，在大多数情况下，不同的DR等位基因识别的核心区域几乎相同，尽管有所不同，这表明不同的DR等位基因可能识别其肽配体上的相似结构。此外，还发现这些核心区域尽管源自不相关序列，但具有共同的结构模式。当仔细研究其他几个不相关决定簇的序列时，发现所确定的结构基序在一些良好的DR结合物中存在，但在其他一些良好的DR结合物中不存在，这表明肽分子的良好DR结合能力可能与不止一种单一序列模式兼容。
