ArticleBiophysical journal2004
SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer?
Article in Biophysical journal, 2004. 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, 57 citations in OpenAlex.
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- Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.Journal of molecular biology · 2020Review
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Transient Secondary Structures as General Target-Binding Motifs in Intrinsically Disordered Proteins.International journal of molecular sciences · 2018Review
- The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Biophysical journal · 2017Article
- Hydrodynamic and Membrane Binding Properties of Purified Rous Sarcoma Virus Gag Protein.Journal of virology · 2015Article
- Probing the average local structure of biomolecules using small-angle scattering and scaling laws.Biophysical journal · 2014Article
- Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy.Journal of Raman spectroscopy : JRS · 2013Article
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- How random are intrinsically disordered proteins? A small angle scattering perspective.Current protein & peptide science · 2012Review
- Understanding the structural ensembles of a highly extended disordered protein.Molecular bioSystems · 2012Article
- Central domain deletions affect the SAXS solution structure and function of yeast Hsp40 proteins Sis1 and Ydj1.BMC structural biology · 2011Article
- ATP induces conformational changes in the carboxyl-terminal region of ClC-5.The Journal of biological chemistry · 2011Article
- Analysis of PKR structure by small-angle scattering.Journal of molecular biology · 2009Article
- Chain dynamics of nascent polypeptides emerging from the ribosome.ACS chemical biology · 2008Article
- Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3.Biophysical journal · 2008Article
- Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.Journal of molecular biology · 2007Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Grb14 belongs to the Grb7 family of adapters and was identified as a negative regulator of insulin signal transduction. Between the PH (pleckstrin homology) and SH2 (Src homology 2) domains is a new binding domain implicated in the interaction with receptor tyrosine kinases called PIR (phosphorylated insulin receptor interaction region). Both PIR and SH2 domains interact with the insulin receptor, but their relative role varies considering the member of the Grb7 family and the tyrosine kinase receptor. In the case of Grb14, PIR is the main binding domain and is sufficient to inhibit the insulin receptor kinase activity. We have proposed, on the basis of NMR measurements, that PIR lacks ordered structure and presents a high flexibility, although remaining fully active. To complement this first study, we have used small-angle x-ray scattering in solution together with a modeling approach representing the PIR domain as a chain of pseudo residues. Circular dichroism experiments were also performed in the presence of variable amounts of trifluoroethanol. These observations, together with an ensemble of sequence analyses and previous NMR results, all support the view of PIR as essentially unstructured but with a potentially structured short stretch encompassing residues 399-407. This stretch, which may be only structured transiently in the isolated molecule, could play a major role in Grb14 PIR binding to a biological partner by undergoing a structural transition.
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