THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS

被引：169
|
作者：
POTTS, BCM
SMITH, J
AKKE, M
MACKE, TJ
OKAZAKI, K
HIDAKA, H
CASE, DA
CHAZIN, WJ
机构：
[1] Scripps Res Inst, RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA
[2] NAGOYA UNIV, SCH MED, DEPT PHARMACOL, NAGOYA, AICHI 466, JAPAN
来源：
NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 09期
关键词：
D O I：
10.1038/nsb0995-790
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 S100 calcium-binding proteins are implicated as effecters in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.
引用
收藏
页码：790 / 796
页数：7
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