Modeling and Structure Determination of Homo-Oligomeric Proteins: An Overview of Challenges and Current Approaches.

ABSTRACT: Protein homo-oligomerization is a very common phenomenon, and approximately half of proteins form homo-oligomeric assemblies composed of identical subunits. The vast majority of such assemblies possess internal symmetry which can be either exploited to help or poses challenges during structure determination. Moreover, aspects of symmetry are critical in the modeling of protein homo-oligomers either by docking or by homology-based approaches. Here, we first provide a brief overview of the nature of protein homo-oligomerization. Next, we describe how the symmetry of homo-oligomers is addressed by crystallographic and non-crystallographic symmetry operations, and how biologically relevant intermolecular interactions can be deciphered from the ordered array of molecules within protein crystals

SUBMITTER: Gaber A 

PROVIDER: S-EPMC8396596 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature