人上皮粘蛋白核心肽片段中的二级结构元件
Elements of secondary structure in a human epithelial mucin core peptide fragment.
作者信息
Tendler S J
机构信息
Department of Pharmaceutical Sciences, University of Nottingham, U.K.
出版信息
Biochem J. 1990 May 1;267(3):733-7. doi: 10.1042/bj2670733.
Abstract
The protein core of human epithelial mucin has previously been shown to consist of tandem repeats of a 20-amino-acid sequence that carries the epitopes for a number of tumour-marking monoclonal antibodies. High-field n.m.r. studies have now been undertaken on an 11-amino-acid fragment of this sequence dissolved in dimethyl sulphoxide. The studies reveal elements of secondary structure to be present: a type I beta-turn has been identified from Asp2 to Arg4 of this peptide, and this turn is extended by Pro5 being in the trans form. The observed turn region extends into the known epitopes for the antibodies C595 and NCRC-11 and may form the basis for how the antibodies recognize these peptides.
摘要
人上皮粘蛋白的蛋白质核心先前已被证明由一个20个氨基酸序列的串联重复组成，该序列带有许多肿瘤标记单克隆抗体的表位。现已对溶解在二甲基亚砜中的该序列的一个11个氨基酸片段进行了高场核磁共振研究。研究揭示了二级结构元素的存在：已从该肽的Asp2至Arg4鉴定出一个I型β-转角，并且该转角因Pro5处于反式构象而得以延伸。观察到的转角区域延伸到抗体C595和NCRC-11的已知表位中，并且可能构成抗体识别这些肽的基础。
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