Your browser doesn't support javascript.
loading
Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery.
Born, Alexandra; Nichols, Parker J; Henen, Morkos A; Chi, Celestine N; Strotz, Dean; Bayer, Peter; Tate, Shin-Ichi; Peng, Jeffrey W; Vögeli, Beat.
Afiliación
  • Born A; Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA.
  • Nichols PJ; Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA.
  • Henen MA; Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA.
  • Chi CN; Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt.
  • Strotz D; Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, 75123, Uppsala, Sweden.
  • Bayer P; Laboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zurich, Switzerland.
  • Tate SI; Strukturelle und Medizinische Biochemie, Universität Duisburg-Essen, Universitätsstrasse 2-5, 45117, Essen, Germany.
  • Peng JW; Department of Mathematical and Life Sciences, Hiroshima University, Hiroshima, Japan.
  • Vögeli B; Department of Chemistry and Biochemistry & Department of Physics, University of Notre Dame, Notre Dame, IN, 46556, USA.
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.
Asunto(s)
Palabras clave
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

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
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

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