Structure of the heterodimeric complex between CAD domains of CAD and ICAD

被引：59

作者：

Otomo, T

Sakahira, H

Uegaki, K

Nagata, S

Yamazaki, T

机构：

[1] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan

[2] Osaka Univ, Sch Med, Dept Genet, Suita, Osaka 5650871, Japan

[3] AIST, Osaka Natl Res Inst, Osaka 5638577, Japan

来源：

NATURE STRUCTURAL BIOLOGY | 2000年 / 7卷 / 08期

基金：

日本学术振兴会;

关键词：

D O I：

10.1038/77957

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：

We present here the structure of the complex between the CAD domain of caspase activated deoxyribonuclease (CAD) and the CAD domain of its inhibitor (ICAD), determined by nuclear magnetic resonance spectroscopy. The two domains adopt a very similar fold, which consists of an alpha-helix and a beta-sheet, and are aligned side by side in the complex. Notably the positive charges on the strand beta 2 at one end of the beta-sheet of CAD and negative charges around the opposite end of the beta-sheet of ICAD are paired in the complex. Point mutations of the charged amino acids at this interface, on either CAD or ICAD, prevented formation of the functional CAD-ICAD complex. This implies that the interaction between the CAD domains of CAD and ICAD is an essential step in the correct folding of CAD in the complex.

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页码：658 / 662

页数：5

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