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PDB_Amyloid: an extended live amyloid structure list from the PDB
Kristóf Takács1, Bálint Varga1, Vince Grolmusz1,2
1PIT Bioinformatics Group Eötvös University Budapest Hungary.
FEBS Open Bio
|January 18, 2019
Summary
Researchers developed an automated web server to identify amyloid structures within the Protein Data Bank (PDB). This tool also finds globular proteins with amyloid-like substructures, aiding in the study of protein aggregation.
Area of Science:
- Structural Biology
- Biophysics
- Computational Biology
Background:
- The Protein Data Bank (PDB) houses over 135,000 entries, but few amyloid structures are available due to insolubility.
- Amyloid structures in the PDB are primarily derived from solid-state Nuclear Magnetic Resonance (NMR) data.
- Identifying amyloid structures and similar motifs in large protein databases presents a significant challenge.
Purpose of the Study:
- To create an automatically updated web server for identifying deposited amyloid structures in the PDB.
- To discover globular proteins containing amyloid-like substructures using geometric criteria.
- To provide a regularly updated resource for researchers studying protein aggregation and amyloid formation.
Main Methods:
- Geometric analysis of deposited protein structures in the PDB.
- Development of an automated web server to apply geometric conditions for structure identification.
- Literature review to validate the amyloid-forming propensity of identified globular proteins.
Main Results:
- Successfully identified deposited amyloid structures and globular proteins with amyloid-like substructures based on geometric properties.
- Demonstrated that specific geometric conditions are sufficient for identifying these structures.
- Found evidence that many identified globular proteins are prone to forming amyloids.
Conclusions:
- The developed web server effectively identifies amyloid and partial amyloid structures within the PDB.
- Geometric analysis is a powerful method for detecting amyloidogenic regions in proteins.
- The findings contribute to a better understanding of protein aggregation and provide a valuable resource for further research.
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