Intrinsic Disorder in Protein Interactions: Insights From a Comprehensive Structural Analysis
2009

Intrinsic Disorder in Protein Interactions

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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)

10.1371/journal.pcbi.1000316

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