OB-fold domains: a snapshot of the evolution of sequence, structure and function
OB-fold domains: a snapshot of the evolution of sequence, structure and function
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DOI：
10.1016/s0959-440x(02)00392-5
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发表时间：
2002-12-01
影响因子：
6.8
通讯作者：
Arcus, V
中科院分区：
文献类型：
--
作者：
Arcus, V
OB-fold在所有三个领域都有发现，并且在序列和结构数据库中都有很好的代表。OB-折叠是一个五链封闭的P桶，大多数OB-折叠蛋白质使用相同的面进行配体结合或作为活性位点。不同的OB-折叠蛋白质使用这种“折叠相关结合面”来不同地结合寡糖、寡核苷酸、蛋白质、金属离子和催化底物。最近，一些新的结构与OB-折叠已被报道，增加了这组蛋白质的变化，同时保存的特征折叠和结合面。许多结构之间折叠和功能结合面的保守性为研究序列、结构和功能的进化轨迹提供了模型。
The OB-fold is found in all three kingdoms and is well represented in both sequence and structural databases. The OB-fold is a five-stranded closed P barrel and the majority of OB-fold proteins use the same face for ligand binding or as an active site. Different OB-fold proteins use this 'fold-related binding face' to, variously, bind oligosaccharides, oligonucteotides, proteins, metal ions and catalytic substrates. Recently, a number of new structures with OB-folds have been reported that augment the variation seen for this set of proteins whilst conserving the characteristic fold and binding face. The conservation of fold and a functional binding face amongst many structures provides a model for investigating the evolutionary trajectory of sequence, structure and function.