A model for target protein binding to calcium-activated S100 dimers

被引：18

作者：

Groves, P

Finn, BE

Kuznicki, J

Forsén, S

机构：

[1] M Nencki Inst Expt Biol, Dept Mol & Cellular Neurobiol, PL-02093 Warsaw, Poland

[2] Univ Lund, Ctr Chem & Chem Engn, Dept Phys Chem 2, S-22100 Lund, Sweden

来源：

FEBS LETTERS | 1998年 / 421卷 / 03期

关键词：

S100; calcium-binding protein; protein structure; target protein binding;

D O I：

10.1016/S0014-5793(97)01535-4

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：

S100 proteins are a family of dimeric calcium-binding proteins implicated in several cancers and neurological diseases. Calbindin D-9k is an unusual monomeric member of the S100 family. A calbindin D-9k mutant containing a novel calcium-induced helix is characterized. Based on sequence comparison, this helix could be a component of other S100 proteins and a factor in target protein binding. The origin of structural differences between three reported apo S100 dimer structures is verified. We conclude that the differences are a result of modeling rather than a function of different target binding properties. A mechanism for target protein binding is suggested. (C) 1998 Federation of European Biochemical Societies.

引用

页码：175 / 179

页数：5

共 20 条

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