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

页码：790 / 796

页数：7

共 47 条

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