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Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery
Univ Colorado, Dept Biochem & Mol Genet, Anschutz Med Campus,12801 East 17th Ave, Aurora, CO 80045 USA.ORCID iD: 0000-0001-8258-0982
Univ Colorado, Dept Biochem & Mol Genet, Anschutz Med Campus,12801 East 17th Ave, Aurora, CO 80045 USA.ORCID iD: 0000-0003-1930-6408
Univ Colorado, Dept Biochem & Mol Genet, Anschutz Med Campus,12801 East 17th Ave, Aurora, CO 80045 USA;Mansoura Univ, Fac Pharm, Mansoura 35516, Egypt.ORCID iD: 0000-0003-4835-5583
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.ORCID iD: 0000-0003-4154-2378
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2019 (English)In: Biomolecular NMR Assignments, ISSN 1874-2718, E-ISSN 1874-270X, Vol. 13, no 1, p. 85-89Article in journal (Refereed) Published
Abstract [en]

Pin1 is a human peptidyl-prolyl cis-trans isomerase important for the regulation of phosphoproteins that are implicated in many diseases including cancer and Alzheimer's. Further biophysical study of Pin1 will elucidate the importance of the two-domain system to regulate its own activity. Here, we report near-complete backbone and side-chain H-1, C-13 and N-15 NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics.

Place, publisher, year, edition, pages
SPRINGER , 2019. Vol. 13, no 1, p. 85-89
Keywords [en]
Pin1, Prolyl isomerase, NMR, Chemical shift assignments, Allostery
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-382507DOI: 10.1007/s12104-018-9857-9ISI: 000463649500018PubMedID: 30353504OAI: oai:DiVA.org:uu-382507DiVA, id: diva2:1308068
Available from: 2019-04-30 Created: 2019-04-30 Last updated: 2019-04-30Bibliographically approved

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Chi, Celestine N.

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Born, AlexandraNichols, Parker J.Henen, Morkos A.Chi, Celestine N.Bayer, PeterVögeli, Beat
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