Beta-strand interfaces of non-dimeric protein oligomers are characterized by scattered charged residue patterns.

ABSTRACT: Protein oligomers are formed either permanently, transiently or even by default. The protein chains are associated through intermolecular interactions constituting the protein interface. The protein interfaces of 40 soluble protein oligomers of stœchiometries above two are investigated using a quantitative and qualitative methodology, which analyzes the x-ray structures of the protein oligomers and considers their interfaces as interaction networks. The protein oligomers of the dataset share the same geometry of interface, made by the association of two individual β-strands (β-interfaces), but are otherwise unrelated. The results show that the β-interfaces are made of two interdigitated interaction networks. One of them involves interactions between main chain atoms (backbone network) whil

SUBMITTER: Feverati G 

PROVIDER: S-EPMC3322119 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature