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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
Published on: August 9, 2019
Conformation of polypyrimidine tract binding protein in solution
Maxim V Petoukhov1, Tom P Monie, Frédéric H-T Allain
1European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 Hamburg, Germany.
Structure (London, England : 1993)
|June 13, 2006
Summary
The polypyrimidine tract binding protein (PTB) is an RNA binding protein. Small-angle X-ray scattering revealed its low-resolution structure, showing domain interactions crucial for its function.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Polypyrimidine tract binding protein (PTB) regulates alternative splicing and translation initiation.
- High-resolution structures of PTB's RNA recognition motifs (RRMs) exist.
- The low-resolution structure of full-length PTB was previously undetermined.
Purpose of the Study:
- To determine the low-resolution structure of the entire PTB protein.
- To investigate the spatial organization of PTB's RRMs in solution.
- To understand how PTB's domain arrangement influences its function.
Main Methods:
- Small-angle X-ray scattering (SAXS) was employed to study full-length PTB and deletion mutants.
- Ab initio analysis of SAXS data was performed.
- Rigid-body modeling was used, integrating high-resolution RRM structures.
Main Results:
- Full-length PTB and its deletion mutants exist as monomers in solution.
- A consistent low-resolution model of PTB's domain organization was generated.
- Domains 3 and 4 exhibit close contact, while domains 1 and 2 show looser associations.
Conclusions:
- The study provides the first low-resolution structure of full-length PTB.
- PTB's domain arrangement, with specific close and loose contacts, is elucidated.
- This structural information offers insights into PTB's regulatory roles in splicing and translation.
