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A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
mpMoRFsDB: a database of molecular recognition features in membrane proteins
Foivos Gypas1, Georgios N Tsaousis, Stavros J Hamodrakas
1Faculty of Biology, Department of Cell Biology and Biophysics, University of Athens, Panepistimiopolis, Athens 157 01, Greece.
Bioinformatics (Oxford, England)
|July 30, 2013
Summary
This study introduces mpMoRFsDB, a database of membrane proteins with molecular recognition features (MoRFs). It organizes and stores MoRFs in membrane proteins, aiding research into protein-protein interactions.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Molecular recognition features (MoRFs) are intrinsically disordered protein regions that become ordered upon binding.
- MoRFs mediate protein-protein interactions, crucial for cellular functions.
- Membrane proteins, comprising ~30% of proteomes, are vital for cellular processes.
Purpose of the Study:
- To create a comprehensive database of membrane proteins containing MoRFs.
- To classify MoRFs based on secondary structure and location within membrane proteins.
- To provide a resource for studying disorder-based interactions in membrane proteins.
Main Methods:
- Collected and organized data on membrane proteins with MoRFs.
- Classified MoRFs by secondary structure post-binding.
- Determined MoRF positions in transmembrane proteins relative to topology.
- Stored data in a publicly accessible mySQL database with a web interface.
Main Results:
- Identified MoRFs in both transmembrane and peripheral membrane proteins.
- Cataloged MoRF secondary structures and locations.
- Developed a user-friendly interface for database access and visualization.
Conclusions:
- The mpMoRFsDB database offers valuable insights into intrinsically disordered regions in membrane proteins.
- This resource facilitates the study of molecular recognition and protein-protein interactions involving membrane proteins.
- The integrated visualization tools aid in understanding structural dynamics of MoRFs.
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