Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1985 Jul 15;229(2):485-9.
doi: 10.1042/bj2290485.

The role of the phosphate group for the structure of phosphopeptide products of adenosine 3',5'-cyclic monophosphate-dependent protein kinase

R C Hider, U Ragnarsson, O Zetterqvist

The role of the phosphate group for the structure of phosphopeptide products of adenosine 3',5'-cyclic monophosphate-dependent protein kinase

R C Hider et al. Biochem J. .

Abstract

By c.d. studies it is shown that liver-pyruvate-kinase-related peptide substrates of cyclic AMP-dependent protein kinase have a high tendency towards non-random structures in non-aqueous media. When phosphorylated, the conformation tendencies decrease. This structural change is explained in terms of the formation of strong intrapeptide phosphate-guanidinium salt links. It is proposed that similar events occur at the catalytic site of protein kinase and that such an interaction could facilitate the removal of the phosphorylated products.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

References

    1. J Biol Chem. 1977 Jul 25;252(14):4888-94 - PubMed
    1. Biochem Biophys Res Commun. 1976 Jun 7;70(3):696-703 - PubMed
    1. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2551-5 - PubMed
    1. Annu Rev Biochem. 1979;48:923-59 - PubMed
    1. Can J Biochem. 1979 Jun;57(6):789-97 - PubMed

Publication types