Intrinsic Disorder in Protein Interactions
Author Information
Author(s): Fong Jessica H., Shoemaker Benjamin A., Garbuzynskiy Sergiy O., Lobanov Michail Y., Galzitskaya Oxana V., Panchenko Anna R.
Primary Institution: National Center for Biotechnology Information, National Institutes of Health, Bethesda, Maryland, United States of America
Hypothesis
How much intrinsic disorder do protein complexes contain and what is its functional importance?
Conclusion
The study reveals that intrinsic disorder in protein complexes plays a significant role in regulating binding specificity and functionality.
Supporting Evidence
- Disorder in protein complexes is common, with up to one third of residues being disordered.
- Homodimers exhibit significantly higher disorder than heterodimers.
- Disordered regions can regulate binding specificity and influence kinetics.
Takeaway
Some proteins are like squishy toys that can change shape when they connect with other proteins, helping them do their jobs better.
Methodology
A large-scale analysis of disorder using protein structures in complex and unbound forms, focusing on X-ray structures with resolution better than 3Å.
Limitations
The study may not account for all factors influencing disorder, such as crystallization conditions.
Statistical Information
P-Value
1E-8
Statistical Significance
p<0.001
Digital Object Identifier (DOI)
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