人类补体第一成分C1q亚成分A链和B链氨基酸序列的完成。
Completion of the amino acid sequences of the A and B chains of subcomponent C1q of the first component of human complement.
作者信息
Reid K B, Gagnon J, Frampton J
出版信息
Biochem J. 1982 Jun 1;203(3):559-69. doi: 10.1042/bj2030559.
Abstract
The sequences of amino acid residues 109--224 of the A chain, and residues 109--22 of the B chain, of human subcomponent C1q are given. These results, along with previously published sequence data on the N-terminal, collagen-like, regions of the A and B chains [Reid (1979) Biochem. J. 179, 367--371] yield the complete amino acid sequences of the A and B chains of subcomponent C1q. The asparagine residue at position A-124 has been identified as the major site of asparagine-linked carbohydrate in subcomponent C1q. When the sequences of the C-terminal, 135-residue-long, 'globular' regions of A and B chains are compared they show 40% homology. The degree of homology over certain stretches of 15--20 residues, within the C-terminal regions, rises up to values of 73%, indicating the presence of strongly conserved structures. Structure prediction studies indicate that both the A and B chain C-terminal regions may adopt a predominantly beta-type structure with apparently little alpha-helical structure.
摘要
给出了人补体亚成分C1q A链109 - 224位氨基酸残基以及B链109 - 22位氨基酸残基的序列。这些结果，连同先前发表的关于A链和B链N端胶原样区域的序列数据[Reid(1979)《生物化学杂志》179, 367 - 371]，得出了补体亚成分C1q A链和B链的完整氨基酸序列。已确定A - 124位的天冬酰胺残基是补体亚成分C1q中天冬酰胺连接型碳水化合物的主要位点。当比较A链和B链C端135个残基长的“球状”区域的序列时，它们显示出40%的同源性。在C端区域内某些15 - 20个残基的片段上，同源性程度上升至73%，表明存在高度保守的结构。结构预测研究表明，A链和B链的C端区域可能主要采用β型结构，明显几乎没有α螺旋结构。
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