Modeling the structure of SARS 3a transmembrane protein using a minimum unfavorable contact approach.

ABSTRACT: 3a is an accessory protein from SARS coronavirus that is known to play a significant role in the proliferation of the virus by forming tetrameric ion channels. Although the monomeric units are known to consist of three transmembrane (TM) domains, there are no solved structures available for the complete monomer. The present study proposes a structural model for the transmembrane region of the monomer by employing our previously tested approach, which predicts potential orientations of TM α-helices by minimizing the unfavorable contact surfaces between the different TM domains. The best model structure comprising all three α-helices has been subjected to MD simulations to examine its quality. The TM bundle was found to form a compact and stable structure with significant inter

SUBMITTER: Ramakrishna S 

PROVIDER: S-EPMC7090505 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature