Role of the N-terminus in the structure and stability of chicken annexin V

被引：26
|
作者：
Arboledas, D [1 ]
Olmo, N [1 ]
Lizarbe, MA [1 ]
Turnay, J [1 ]
机构：
[1] UNIV COMPLUTENSE MADRID, FAC CIENCIAS QUIM, DEPT BIOQUIM & BIOL MOL, E-28040 MADRID, SPAIN
来源：
FEBS LETTERS | 1997年 / 416卷 / 02期
关键词：
annexin V; calcium binding; circular dichroism spectroscopy; fluorescence emission spectroscopy;
D O I：
10.1016/S0014-5793(97)01207-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The role of the short N-terminal region of chicken annexin V in the maintenance of the protein structure and its influence in the conformation of the calcium binding regions was analyzed. The N-terminal domain is not essential for protein folding, wild-type and dnt-annexin V showing almost identical secondary structures. However, the partial truncation of the N-terminus significantly decreases the melting temperature of the protein and induces the partial exposure of Trp(187) which is normally located in a hydrophobic pocket of the calcium binding region of domain 3 of annexin V in the Ca2+-free form. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码：217 / 220
页数：4
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