α-螺旋卷曲螺旋的结构。

The structure of alpha-helical coiled coils.

作者信息

Lupas Andrei N, Gruber Markus

机构信息

Max-Planck-Institute for Developmental Biology, D-72076 Tübingen, Germany.

出版信息

Adv Protein Chem. 2005;70:37-78. doi: 10.1016/S0065-3233(05)70003-6.

DOI:10.1016/S0065-3233(05)70003-6

PMID:15837513

Abstract

alpha-Helical coiled coils are versatile protein domains, supporting a wide range of biological functions. Their fold is probably better understood than that of any other protein; indeed, uniquely among folds, their structure can be computed from a set of parametric equations. Here, we review the principles of coiled-coil structure, the determinants of their folding and stability, and the diversity of structural forms they assume.

摘要

α-螺旋卷曲螺旋是多功能的蛋白质结构域，支持多种生物学功能。与其他任何蛋白质相比，人们可能对它们的折叠方式了解得更清楚；事实上，在所有折叠结构中，它们的结构独一无二，可以通过一组参数方程计算得出。在这里，我们综述卷曲螺旋结构的原理、其折叠和稳定性的决定因素，以及它们呈现出的结构形式的多样性。