Shin Woong-Hee, Kihara Daisuke
Department of Biological Science, Purdue University, West Lafayette, IN, USA.
Department of Computer Science, Purdue University, West Lafayette, IN, USA.
Methods Mol Biol. 2019;1958:1-13. doi: 10.1007/978-1-4939-9161-7_1.
The Rossmann fold is one of the most commonly observed structural domains in proteins. The fold is composed of consecutive alternating β-strands and α-helices that form a layer of β-sheet with one (or two) layer(s) of α-helices. Here, we will discuss the Rossmann fold starting from its discovery 55 years ago, then overview entries of the fold in the major protein classification databases, SCOP and CATH, as well as the number of the occurrences of the fold in genomes. We also discuss the Rossmann fold as an interesting target of protein engineering as the site-directed mutagenesis of the fold can alter the ligand-binding specificity of the structure.
罗斯曼折叠是蛋白质中最常见的结构域之一。该折叠由连续交替的β链和α螺旋组成，形成一层β折叠片层以及一层（或两层）α螺旋。在此，我们将从55年前罗斯曼折叠的发现开始讨论，然后概述其在主要蛋白质分类数据库SCOP和CATH中的条目，以及该折叠在基因组中的出现次数。我们还将讨论罗斯曼折叠作为蛋白质工程的一个有趣靶点，因为对该折叠进行定点诱变可以改变其结构的配体结合特异性。
