Abstract
Membrane proteins play a variety of biological functions to the survival of organisms and functionalities of these proteins are often due to their homo- or hetero-complexation. Encoded by ~30% of the genome in most organisms, they represent the target of over half of nowadays drugs. Spanning the entirety of the cell membrane, transmembrane proteins are the most common type of membrane proteins and can be classified by secondary structures: alpha-helical and beta-barrel structures. Protein-protein interaction (PPI) have been widely studied for globular proteins and many computational tools are available for predicting PPI sites and construct models of complexes. Here, the structural regions of a non-redundant set of 232 alpha-helical and 37 beta-barrel transmembrane complexes and their interfaces are analyzed. Using the residue composition, frequency and propensity, this study brings the light on the marker residue types located at the structural regions of alpha-helical and beta-barrel transmembrane homomeric protein complexes and of their interfaces. This study also shows the necessity to relate the frequency to the composition into a ratio for immediately figuring out residue types presenting high frequencies at the interface and/or at one of its structural regions despite being a minor contributor compared to other residue types to that location's residue composition.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.