Substrate and pseudosubstrate interactions with protein kinases: determinants of specificity - PubMed (original) (raw)
Review
Substrate and pseudosubstrate interactions with protein kinases: determinants of specificity
B E Kemp et al. Trends Biochem Sci. 1994 Nov.
Abstract
Protein crystallography has revealed that protein kinases have extended protein-substrate-binding grooves associated with their active sites. Some protein kinases are autoinhibited by a mechanism in which part of their structure, termed a pseudosubstrate, occupies the active site. Substrates and pseudosubstrates occupy overlapping regions within the extended substrate-binding groove, making multiple specific electrostatic and non-polar contacts. With masterly economy, Nature has exploited the active site in many protein kinases to both recognize substrates with great specificity and autoregulate by remaining inactive until the appropriate activation signal is received.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources