Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery.
Biomol NMR Assign
; 13(1): 85-89, 2019 04.
Article
em En
| MEDLINE
| ID: mdl-30353504
ABSTRACT
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 1H, 13C and 15N NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics.
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Base de dados:
MEDLINE
Assunto principal:
Apoproteínas
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Fosfoproteínas
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Ressonância Magnética Nuclear Biomolecular
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Peptidilprolil Isomerase de Interação com NIMA
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article