Serine-53 at the Tip of the Glycine-Rich Loop of cAMP-Dependent Protein Kinase: Role in Catalysis, P-Site Specificity, and Interaction with Inhibitors
Author:
Affiliation:
1. Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of California−San Diego, La Jolla, California 92093-0654
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi992800w
Reference45 articles.
1. Kinetic Analyses of Mutations in the Glycine-Rich Loop of cAMP-Dependent Protein Kinase
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3. cAMP-DEPENDENT PROTEIN KINASE: FRAMEWORK FOR A DIVERSE FAMILY OF REGULATORY ENZYMES
4. The glycine-rich sequence of protein kinases: a multifunctional element
5. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with magnesium-ATP and peptide inhibitor
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