The kinetics of the interaction between cyclic AMP and the regulatory moiety of protein kinase II

Øgreid, D; Døskeland, Stein Ove

doi:10.1016/0014-5793(81)80184-6

Cited by 43 publications

(33 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The nucleotide bound more rapidly to site A than to site B of the free RII, the initial rate of accumulation to either site was linear, and the apparent association rate constant (k,) was independent of the contration of cyclic AMP [9].…”

Section: Discussionmentioning

confidence: 98%

“…Some aspects of the interaction between cyclic AMP and site A and B of the free regulatory moiety (RR) of protein kinase II (cAKI1) were presented in [9]. The nucleotide bound more rapidly to site A than to site B of the free RII, the initial rate of accumulation to either site was linear, and the apparent association rate constant (k,) was independent of the contration of cyclic AMP [9].…”

Section: Discussionmentioning

confidence: 99%

“…Other reagents were from the sources in [3,9]. Buffer A is 15 mM Hepes-NaOH(pH 7.0) containing 0.3 mM EGTA, 0.1 mM EDTA and 20 mM 2-mercaptoethanol.…”

Section: Elsevierjnorth-hoiland Biomedical Pressmentioning

confidence: 99%

“…Buffer B is 62.5 mM Hepes-NaOH (pH 7 .O) containing 4 M NaCl, 37.5 mM EDTA, 0.5 mM dithiothreitol, 20 mM 2-mercaptoethanol, 0.5 mg bovine serum albumin/ml and 0.2 mg heat-stable protein fraction/ml [9].…”

Section: Elsevierjnorth-hoiland Biomedical Pressmentioning

confidence: 99%

See 3 more Smart Citations

The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium

Øgreid¹,

Døskeland²

1981

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

“…Other reagents were from the sources in [3,9]. Buffer A is 15 mM Hepes-NaOH(pH 7.0) containing 0.3 mM EGTA, 0.1 mM EDTA and 20 mM 2-mercaptoethanol.…”

Section: Elsevierjnorth-hoiland Biomedical Pressmentioning

confidence: 99%

Section: Elsevierjnorth-hoiland Biomedical Pressmentioning

confidence: 99%

See 2 more Smart Citations

The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium

Øgreid¹,

Døskeland²

1981

FEBS Letters

Self Cite

View full text Add to dashboard Cite

“…Instead, its role is to modulate access of cAMP to domain A and to contribute cooperativity to the activation process. In the holoenzyme, only domain B is accessible (10,11). cAMP thus binds first to domain B, which induces a conformational change.…”

mentioning

confidence: 99%

Dissecting cAMP Binding Domain A in the RIα Subunit of cAMP-dependent Protein Kinase

Huang

Taylor

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

The two gene-duplicated cAMP binding domains in the regulatory subunits of cAMP dependent protein kinase are each comprised of an A helix, an eight-stranded ␤-barrel, and a B and C helix (1). The A domain is required for high affinity binding to C, while the B domain regulates access to the A domain. Using a combination of a yeast two-hybrid screen coupled with deletion analysis, cAMP binding domain A of R I was dissected into two structurally and functionally distinct subsites, one that binds cAMP and another that binds the C subunit. The minimum stable subdomain required for binding to C in the 1-3 micromolar range is composed of residues 94 -169, while residues 236 -244, mapped to the C helix of cAMP binding domain A, were defined as a second surface necessary for high affinity (5-10 nanomolar) binding to C. This portion of the C helix, due to its position directly between the two subsites, serves as a molecular switch for either a cAMP-bound conformation or a Cbound conformation and can thus modulate interactions of cAMP binding domain A with cAMP, with C, and with cAMP binding domain B.

show abstract

Biochemical Networks in Psychiatric Disease

Lindskog

Halnes

Oliveira

et al. 2010

Systems Biology in Psychiatric Research

View full text Add to dashboard Cite

The kinetics of the interaction between cyclic AMP and the regulatory moiety of protein kinase II

Cited by 43 publications

References 8 publications

The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium

The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium

Dissecting cAMP Binding Domain A in the RIα Subunit of cAMP-dependent Protein Kinase

Biochemical Networks in Psychiatric Disease

Contact Info

Product

Resources

About