An analysis of oligomerization interfaces in transmembrane proteins.

ABSTRACT:

Background

The amount of transmembrane protein (TM) structures solved to date is now large enough to attempt large scale analyses. In particular, extensive studies of oligomeric interfaces in the transmembrane region are now possible.

Results

We have compiled the first fully comprehensive set of validated transmembrane protein interfaces in order to study their features and assess what differentiates them from their soluble counterparts.

Conclusions

The general features of TM interfaces do not differ much from those of soluble proteins: they are large, tightly packed and possess many interface core residues. In our set, membrane lipids were not found to significantly mediate protein-protein interfaces. Although no G protein-coupled receptor (GPCR) was included in the

SUBMITTER: Duarte JM 

PROVIDER: S-EPMC4015793 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature