人低分子量激肽原中二硫键的排列
Arrangement of the disulphide bridges in human low-Mr kininogen.
作者信息
Kellermann J, Thelen C, Lottspeich F, Henschen A, Vogel R, Müller-Esterl W
机构信息
Max-Planck-Institute for Biochemistry, Martinsried, Federal Republic of Germany.
出版信息
Biochem J. 1987 Oct 1;247(1):15-21. doi: 10.1042/bj2470015.
Abstract
The arrangement of the disulphide bridges in human low-Mr kininogen has been elucidated. Low-Mr kininogen contains 18 half-cystine residues forming nine disulphide bridges. The first and the last half-cystine residues of the amino acid sequence form a disulphide loop which spans the heavy- and the light-chain portion of the kininogen molecule. The other 16 half-cystine residues are linked consecutively to form eight loops of 4-20 amino acids; these loops are lined up in the heavy-chain portion of the kininogen molecule. In this way, a particular pattern of disulphide loops is formed which seems to be of critical importance for the inhibitor function of human kininogen.
摘要
人低分子量激肽原中二硫键桥的排列已被阐明。低分子量激肽原含有18个半胱氨酸残基，形成9个二硫键桥。氨基酸序列的第一个和最后一个半胱氨酸残基形成一个二硫键环，该环跨越激肽原分子的重链和轻链部分。其他16个半胱氨酸残基连续相连，形成8个由4 - 20个氨基酸组成的环；这些环排列在激肽原分子的重链部分。通过这种方式，形成了一种特定的二硫键环模式，这似乎对人激肽原的抑制功能至关重要。
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