Solution structure of a cysteine rich domain of rat protein kinase C.
Nat Struct Biol
; 1(6): 383-7, 1994 Jun.
Article
in En
| MEDLINE
| ID: mdl-7664052
ABSTRACT
Intracellular protein phosphorylation by protein kinase C (PKC) plays a major role in the translation of extracellular signals into cellular events. Speculations on the structural basis for PKC activation are based on sequence homology between their cysteine-rich domains (CRD) and the DNA-binding 'zinc-fingers'. We produced a fragment comprising the second CRD (CRD2) of rat PKC-alpha and determined its three-dimensional structure in solution by NMR spectroscopy. This revealed that CRD2 adopts a globular fold allowing two non-consecutive sets of zinc-binding residues to form two separate metal-binding sites. The fold is different to those previously proposed and allows insight into the molecular topology of a family of homologous proteins.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Conformation
/
Protein Kinase C
/
Models, Molecular
/
Cell Cycle Proteins
Type of study:
Prognostic_studies
Limits:
Animals
/
Humans
Language:
En
Journal:
Nat Struct Biol
Journal subject:
BIOLOGIA MOLECULAR
Year:
1994
Document type:
Article
Affiliation country:
Switzerland
Publication country:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA