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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Local structural disorder imparts plasticity on linear motifs
Monika Fuxreiter1, Peter Tompa, István Simon
1Institute of Enzymology, BRC, Hungarian Academy of Sciences, Budapest, Hungary.
Bioinformatics (Oxford, England)
|March 28, 2007
Summary
Linear motifs (LMs) mediating protein interactions are often found in disordered protein regions. These flexible motifs combine ordered specificity residues with disordered carriers for transient molecular switches.
Area of Science:
- Molecular Biology
- Biophysics
- Bioinformatics
Background:
- Protein interaction networks rely on dynamic molecular switches.
- Linear motifs (LMs) are short, variable recognition segments.
- LMs are often located in intrinsically disordered regions.
Purpose of the Study:
- To investigate the prevalence of intrinsic disorder in LM-containing proteins.
- To understand the structural properties of LMs.
- To connect LM characteristics with intrinsically unstructured proteins (IUPs).
Main Methods:
- Analysis of LM-containing proteins from the Eukaryotic Linear Motif (ELM) database.
- Prediction of intrinsic disorder for LM-containing proteins.
- Amino acid composition and property analysis.
Main Results:
- LMs are predominantly embedded in locally unstructured protein regions.
- LM amino acid composition shows a mix of folded and disordered protein characteristics.
- LMs utilize ordered residues on flexible carriers for binding.
Conclusions:
- LMs are intrinsically disordered elements, facilitating transient molecular recognition.
- This structural feature links LMs to the binding mechanisms of IUPs.
- LMs play a role in regulatory functions through non-conventional binding.
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