An automatic method for predicting transmembrane protein structures using cryo-EM and evolutionary data.

ABSTRACT: The transmembrane (TM) domains of many integral membrane proteins are composed of alpha-helix bundles. Structure determination at high resolution (<4 A) of TM domains is still exceedingly difficult experimentally. Hence, some TM-protein structures have only been solved at intermediate (5-10 A) or low (>10 A) resolutions using, for example, cryo-electron microscopy (cryo-EM). These structures reveal the packing arrangement of the TM domain, but cannot be used to determine the positions of individual amino acids. The observation that typically, the lipid-exposed faces of TM proteins are evolutionarily more variable and less charged than their core provides a simple rule for orienting their constituent helices. Based on this rule, we developed score functions and automated methods for orienti

SUBMITTER: Fleishman SJ 

PROVIDER: S-EPMC1304811 | biostudies-literature | 2004 Nov

REPOSITORIES: biostudies-literature