ArticleProtein science : a publication of the Protein Society2009
Residual structure within the disordered C-terminal segment of p21(Waf1/Cip1/Sdi1) and its implications for molecular recognition.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 34 citations in OpenAlex.
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- The activity and stability of the intrinsically disordered Cip/Kip protein family are regulated by non-receptor tyrosine kinases.Journal of molecular biology · 2015Article
- Using chemical shifts to generate structural ensembles for intrinsically disordered proteins with converged distributions of secondary structure.Intrinsically disordered proteins · 2015Article
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- Comparison of structure determination methods for intrinsically disordered amyloid-β peptides.The journal of physical chemistry. B · 2014Article
- Coupled folding and binding of the disordered protein PUMA does not require particular residual structure.Journal of the American Chemical Society · 2014Article
- The Stress-response protein prostate-associated gene 4, interacts with c-Jun and potentiates its transactivation.Biochimica et biophysica acta · 2014Article
- A novel method of predicting protein disordered regions based on sequence features.BioMed research international · 2013Article
- Cell cycle regulation by the intrinsically disordered proteins p21 and p27.Biochemical Society transactions · 2012Review
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- Intramolecular interactions stabilizing compact conformations of the intrinsically disordered kinase-inhibitor domain of Sic1: a molecular dynamics investigation.Frontiers in physiology · 2012Article
- Constructing ensembles for intrinsically disordered proteins.Current opinion in structural biology · 2011Review
- Anchoring intrinsically disordered proteins to multiple targets: lessons from N-terminus of the p53 protein.International journal of molecular sciences · 2011Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Probably the most unusual class of proteins in nature is the intrinsically unstructured proteins (IUPs), because they are not structured yet play essential roles in protein-protein signaling. Many IUPs can bind different proteins, and in many cases, adopt different bound conformations. The p21 protein is a small IUP (164 residues) that is ubiquitous in cellular signaling, for example, cell cycle control, apoptosis, transcription, differentiation, and so forth; it binds to approximately 25 targets. How does this small, unstructured protein recognize each of these targets with high affinity? Here, we characterize residual structural elements of the C-terminal segment of p21 encompassing residues 145-164 using a combination of NMR measurements and molecular dynamics simulations. The N-terminal half of the peptide has a significant helical propensity which is recognized by calmodulin while the C-terminal half of the peptide prefers extended conformations that facilitate binding to the proliferating cell nuclear antigen (PCNA). Our results suggest that the final bound conformations of p21 (145-164) pre-exist in the free peptide even without its binding partners. While the conformational flexibility of the p21 peptide is essential for adapting to diverse binding environments, the intrinsic structural preferences of the free peptide enable promiscuous yet high affinity binding to a diverse array of molecular targets.
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