Occupational hazards: allosteric regulation of protein kinases through the nucleotide-binding pocket.
Biochem Soc Trans
; 39(2): 472-6, 2011 Apr.
Article
in En
| MEDLINE
| ID: mdl-21428922
ABSTRACT
Targeting the protein kinase ATP-binding pocket provides a significant opportunity for the treatment of disease. Recent studies have revealed a central activity-independent role for nucleotide pocket occupation in the allosteric behaviour of diverse kinases. Regulation of nucleotide pocket conformation with either nucleotides or ATP competitive inhibitors has revealed an added dimension to the targeting of kinases. In the present paper, using PKC (protein kinase C) as a paradigm, the liabilities and opportunities associated with the occupation of the nucleotide pocket are explored.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Kinases
/
Binding, Competitive
/
Allosteric Regulation
/
Nucleotides
Limits:
Animals
/
Humans
Language:
En
Journal:
Biochem Soc Trans
Year:
2011
Document type:
Article
Affiliation country: