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Principles and characteristics of biological assemblies in experimentally determined protein structures.
Current opinion in structural biology Pub Date : 2019-04-06 , DOI: 10.1016/j.sbi.2019.03.006
Qifang Xu 1 , Roland L Dunbrack 1
Affiliation  

More than half of all structures in the PDB are assemblies of two or more proteins, including both homooligomers and heterooligomers. Structural information on these assemblies comes from X-ray crystallography, NMR, and cryo-EM spectroscopy. The correct assembly in an X-ray structure is often ambiguous, and computational methods have been developed to identify the most likely biologically relevant assembly based on physical properties of assemblies and sequence conservation in interfaces. Taking advantage of the large number of structures now available, some of the most recent methods have relied on similarity of interfaces and assemblies across structures of homologous proteins.

中文翻译:

实验确定的蛋白质结构中生物组装的原理和特征。

PDB 中超过一半的结构是两种或多种蛋白质的组装体,包括同源寡聚体和异源寡聚体。这些组件的结构信息来自 X 射线晶体学、核磁共振和低温电磁波谱。X 射线结构中的正确组装通常是模棱两可的,并且已经开发了计算方法来根据组装的物理特性和界面中的序列守恒来识别最可能的生物学相关组装。利用现在可用的大量结构,一些最新的方法依赖于同源蛋白质结构之间界面和组装的相似性。
更新日期:2019-11-01
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