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
en En
| MEDLINE
| ID: mdl-30353504
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Apoproteínas
/
Fosfoproteínas
/
Resonancia Magnética Nuclear Biomolecular
/
Peptidilprolil Isomerasa de Interacción con NIMA
Límite:
Humans
Idioma:
En
Revista:
Biomol NMR Assign
Asunto de la revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Año:
2019
Tipo del documento:
Article
País de afiliación:
Estados Unidos