ElGamacy Mohammad, Hernandez Alvarez Birte
Systems Biology of Development Group, Friedrich Miescher Laboratory of the Max Planck Society, Max-Planck-Ring 9, Tübingen, 72076, Germany; Division of Translational Oncology, Department of Hematology, Oncology, Clinical Immunology and Rheumatology, University Hospital Tübingen, Otfried-Müller-Strasse 10, Tübingen, 72076, Germany; Department of Protein Evolution, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, Tübingen, 72076, Germany.
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Max-Planck-Ring 5, Tübingen, 72076, Germany.
Curr Opin Struct Biol. 2021 Jun;68:224-234. doi: 10.1016/j.sbi.2021.03.011. Epub 2021 May 5.
Natural helical bundles (HBs) constitute a ubiquitous class of protein folds built of two or more longitudinally arranged α-helices. They adopt topologies that include symmetric, highly regular assemblies all the way to asymmetric, loosely packed domains. The diverse functional spectrum of HBs ranges from structural scaffolds to complex and dynamic effectors as molecular motors, signaling and sensing molecules, enzymes, and molecular switches. Symmetric HBs, particularly coiled coils, offer simple model systems providing an ideal entry point for protein folding and design studies. Herein, we review recent progress unveiling new structural features and functional mechanisms in natural HBs and cover staggering advances in the de novo design of HBs, giving rise to exotic structures and the creation of novel functions.
天然螺旋束（HBs）是一类普遍存在的蛋白质折叠结构，由两个或更多纵向排列的α螺旋组成。它们具有多种拓扑结构，从对称的、高度规则的组装体到不对称的、松散堆积的结构域。HBs的功能谱多样，涵盖从结构支架到作为分子马达、信号和传感分子、酶以及分子开关的复杂动态效应器。对称的HBs，特别是卷曲螺旋，提供了简单的模型系统，为蛋白质折叠和设计研究提供了理想的切入点。在此，我们综述了揭示天然HBs新结构特征和功能机制的最新进展，并介绍了HBs从头设计方面的惊人进展，这些进展产生了奇特的结构并创造了新的功能。
