P. Wright

Publications557
h-index111
Citations51,823
Highly Influential Citations1,815
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Intrinsically unstructured proteins and their functions
TLDR
Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold, whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.
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Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
TLDR
Many proteins that lack intrinsic globular structure under physiological conditions have now been recognized, and it appears likely that their rapid turnover, aided by their unstructured nature in the unbound state, provides a level of control that allows rapid and accurate responses of the cell to changing environmental conditions.
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Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions
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Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d
The tandem zinc finger (TZF) domain of the protein TIS11d binds to the class II AU-rich element (ARE) in the 3′ untranslated region (3′ UTR) of target mRNAs and promotes their deadenylation and…
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Classification of Intrinsically Disordered Regions and Proteins
TLDR
Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes and is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood.
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Coupling of folding and binding for unstructured proteins.
  • H. Dyson, P. Wright
  • Biology, Chemistry
    Current opinion in structural biology
  • 1 February 2002
View on PubMed
Intrinsically disordered proteins in cellular signalling and regulation
TLDR
Experimental, computational and bioinformatic analyses combine to identify and characterize disordered regions of proteins, leading to a greater appreciation of their widespread roles in biological processes.
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Zinc finger proteins: new insights into structural and functional diversity.
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Linking folding and binding.
  • P. Wright, H. Dyson
  • Biology, Chemistry
    Current opinion in structural biology
  • 1 February 2009
View on PubMed
Mechanism of coupled folding and binding of an intrinsically disordered protein
TLDR
Using NMR titrations and 15N relaxation dispersion, it is shown that the phosphorylated kinase inducible activation domain (pKID) of the transcription factor CREB forms an ensemble of transient encounter complexes on binding to the KIX domain of the CREB binding protein.
View on Nature
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