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

Øgreid, D; Døskeland, Stein Ove

doi:10.1016/0014-5793(81)80185-8

Cited by 68 publications

(39 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, site A differs from site B by having higher rate constants for the association with cyclic AMP as well as for the dissociation of bound nucleotide. The pattern of cyclic AMP association to cAKI1 [3] was very different from that to free RII. The method used to discriminate binding to site A and B (rate of exchange of bound cyclic [ 3H] AMP with excess unlabelled cyclic AMP in 3.2 M NaCl at 0°C conditions that ensure complete dissociation of cAKI1 into free RI1 and C) was identical for the experiments with RI1 and cAKI1.…”

Section: Discussionmentioning

confidence: 67%

“…ammonium-sulphate and bound cyclic [3H]AMP measured [2,5]. As explained in [3] or by including active charcoal (10 mg/ml) or unlabelled cyclic AMP (0.1 mM) in the incubations. In the presence of charcoal and especially at >3O"C, RI1 was unstable unless serum albumin (5 mglml) and heatstable protein (2 mg/ml) were present.…”

Section: Association Rate Studiesmentioning

confidence: 99%

“…The rate of association in the initial phase was the same for all concentrations of RI1 (1 -100 nM) or cyclic [3H]AMP (6-$00 nM) tested. The association rate constant (kf), calculated as explained in [3], was 4 X lo4 M-. s-l for the initial binding to site A and 1.5 X lo4 M-i .…”

Section: The Association Of Cyclic [ 3h]amp and Free Riimentioning

confidence: 99%

“…The procedures for autophosphorylation of cAKI1 and preparation of the catalytic subunit of cAKI1 are described in [3].…”

mentioning

confidence: 99%

See 3 more Smart Citations

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

Øgreid¹,

Døskeland²

1981

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 67%

Section: Association Rate Studiesmentioning

confidence: 99%

Section: The Association Of Cyclic [ 3h]amp and Free Riimentioning

confidence: 99%

“…The procedures for autophosphorylation of cAKI1 and preparation of the catalytic subunit of cAKI1 are described in [3].…”

mentioning

confidence: 99%

See 2 more Smart Citations

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

Øgreid¹,

Døskeland²

1981

FEBS Letters

Self Cite

View full text Add to dashboard Cite

“…It has long been established that the binding affinity of site A is lower than site B, an observation parallel that of the deletion and wild-type CRP, respectively. It is not surprising that cooperativity of ligand binding is different between these two type of sites (35)(36)(37)(38)(39)(40)(41)(42).…”

Section: Discussionmentioning

confidence: 99%

Functional Roles of Loops 3 and 4 in the Cyclic Nucleotide Binding Domain of Cyclic AMP Receptor Protein from Escherichia coli

Chen

Lee

2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Cyclic AMP is a ubiquitous secondary message that regulates a large variety of functions. The protein structural motif that binds cAMP is highly conserved with the exception of loops 3 and 4, whose structure and length are variable. The cAMP receptor protein of Escherichia coli, CRP, was employed as a model system to elucidate the functional roles of these loops. Based on the sequence differences between CRP and cyclic nucleotide gated channel, three mutants of CRP were constructed: deletion (residues 54 -56 in loop 3 were deleted), insertion (loop 4 was lengthened by 5 residues between Glu-78 and Gly-79) and double mutants. The effects of these mutations on the structure and function of CRP were monitored. Results show that the deletion and insertion mutations do not significantly change the secondary structure of CRP, although the tertiary and qua- Cyclic AMP serves as an intracellular message in both prokaryotes and eukaryotes by transmitting information through proteins such as protein kinase A (PKA) 1 , cyclic nucleotidegated ion channels (CNGC), and cAMP receptor protein in Escherichia coli (CRP). These proteins are involved in a very diverse set of cellular functions such as signal transduction, excitability, and gene expression (1-6). These proteins of diverse functions all consist of a cAMP binding motif. The structural motif, which serves as cAMP receptor, is found to display a high degree of similarity. X-ray crystallography and homology modeling results show that, despite obvious divergence of sequence among the receptor domains and significantly different biological functions of these proteins, their CNB domains appear to share a common architecture, all consisting of an ␣-helix (helix A), an eight-stranded ␤-roll, and two more ␣-helices (helices B and C). The body of the CNB pocket is mainly located in the ␤-roll, with the C-helix forming the back of the binding pocket (2,8). The superimposition of the structures of CNB domains from CRP and the regulatory subunits of PKA, as shown below in Fig. 1, indicates that the ␤-roll basically assumes the same structure with the exception of loops 3 and 4 between strands 4 and 5, and strands 6 and 7, respectively. In some cases, such as in CNGC and PKA, loop 3 is shortened whereas loop 4 is lengthened, as shown in Fig. 1. Only six residues (Gly-33, Gly-45, Gly-71, Glu-72, Arg-82, and Ala-84 using the CRP sequence as reference) are invariant among all members of the families. It has been suggested that the invariant residues play important and conserved roles in the folding and function of the CNB sites of these diverse proteins. Gly-33, Gly-45, and Gly-71 are involved in turns between strands of the ␤-roll; Arg-82 and Glu-72 contact the cyclic nucleotide, and the function of Ala-84 is uncertain (3). Despite large variation of primary sequences, the sizes of secondary structural elements of the CNB domain are much conserved among the family. For example, the alignment of CRP and CNGCs by keeping the six conserve residues at the same positions shows that the si...

show abstract

Glucagon Signal‐Transduction Mechanisms

Exton

2001

Comprehensive Physiology

View full text Add to dashboard Cite

The sections in this article are: Glucagon Receptor Regulation of G s Regulation of Adenylate Cyclase Regulation of cAmp‐Dependent Protein Kinase Substrates of cAmp‐Dependent Protein Kinase Mechanisms of Calcium Mobilization Induced by Glucagon Summary

show abstract

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

Cited by 68 publications

References 15 publications

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

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

Functional Roles of Loops 3 and 4 in the Cyclic Nucleotide Binding Domain of Cyclic AMP Receptor Protein from Escherichia coli

Glucagon Signal‐Transduction Mechanisms

Contact Info

Product

Resources

About