ROSETTA-MEMBRANE · Membrane protein structure prediction based on ROSETTA

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Project objective

Integral helical membrane proteins constitute about 20% of all proteins encoded by most genomes and they play crucial role in cell function and communication. In addition, the medical importance of membrane bound receptors, channels, and pumps as targets f or drugs are well established.However, several experimental reasons makes it difficult to obtain the structure of membrane proteins, only 0.6% (168 out of 28,000) of the solved protein structures in the Protein Data Bank (PDB) are membrane proteins. This highlights the need for better and more accurate theoretical structure prediction methods for membrane proteins.Recently, there has been significant progress in structure prediction of globular proteins from sequence (de novo prediction), offering some hope that structure prediction methodology may be able to contribute to the understanding membrane protein structure.In this project, currently the best method to predict the structure of non-membrane proteins, the ROSETTA de novo structure prediction method, will be adapted and optimized to predict the three-dimensional structure of membrane proteins.This project has the potential to significantly enhance the accuracy of the current structural models of membrane proteins (today mostly restricted to 2D topology maps).It also has the potential to provide fundamentally new insights of high biological and biomedical relevance. From a European perspective there is a chance to acquire expertise in an area of key importance in the future.

Original text from CORDIS.

Participants

• STOCKHOLM UNIVERSITY · STOCKHOLMCoordinatorCity levelSweden
• UNIVERSITY OF WASHINGTON · SEATTLEUnited States

Links

• View on CORDIS