Advancing Membrane-Associated Protein Docking with Improved Sampling and Scoring in Rosetta.

ABSTRACT: The oligomerization of protein macromolecules on cell membranes plays a fundamental role in regulating cellular function. From modulating signal transduction to directing immune response, membrane proteins (MPs) play a crucial role in biological processes and are often the target of many pharmaceutical drugs. Despite their biological relevance, the challenges in experimental determination have hampered the structural availability of membrane proteins and their complexes. Computational docking provides a promising alternative to model membrane protein complex structures. Here, we present Rosetta-MPDock, a flexible transmembrane (TM) protein docking protocol that captures binding-induced conformational changes. Rosetta-MPDock samples large conformational ensembles of flexible monomers and do

SUBMITTER: Samanta R 

PROVIDER: S-EPMC12025977 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature