A MODEL STRUCTURE OF THE MUSCLE PROTEIN COMPLEX 4CA2+-CENTER-DOT-TROPONIN-C-CENTER-DOT-TROPONIN-I DERIVED FROM SMALL-ANGLE SCATTERING DATA - IMPLICATIONS FOR REGULATION

被引：100

作者：

OLAH, GA ^{[1
]}

TREWHELLA, J ^{[1
]}

机构：

[1] LOS ALAMOS NATL LAB,DIV CHEM SCI & TECHNOL,LOS ALAMOS,NM 87545

来源：

BIOCHEMISTRY | 1994年 / 33卷 / 43期

关键词：

D O I：

10.1021/bi00209a011

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 report here a model structure for 4Ca(2+)-troponin C-troponin I derived from small-angle X-ray and neutron scattering data using a Monte Carlo modeling method. In this model, troponin I appears as a spiral structure that wraps around 4Ca(2+) troponin C which adopts an extended dumbbell conformation similar to that observed in the crystal structures of troponin C. The troponin I spiral has the approximate dimensions of an alpha-helix and winds through the hydrophobic ''cups'' in each globular domain of troponin C. The model is consistent with a body of previously published biochemical data on the interactions between troponin C and troponin I, and suggests the molecular mechanism for the Ca2+-sensitive switch that regulates the muscle contraction/relaxation cycle involves a signal transmitted via the central spiral region of troponin I.

引用

页码：12800 / 12806

页数：7

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