An active twenty-amino-acid-residue peptide derived from the inhibitor protein of the cyclic AMP-dependent protein kinase

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Bibliographische Detailangaben
Zeitschriftentitel:	Biochemical Journal
Personen und Körperschaften:	Cheng, H C, van Patten, S M, Smith, A J, Walsh, D A
In:	Biochemical Journal, 231, 1985, 3, S. 655-661
Format:	E-Article
Sprache:	Englisch
veröffentlicht:	Portland Press Ltd.
Schlagwörter:	Cell Biology Molecular Biology Biochemistry

Details
Zusammenfassung:	<jats:p>Digestion with Staphylococcus aureus V8 proteinase of the inhibitor protein of the cyclic AMP-dependent protein kinase results in the sequential formation of three active inhibitory peptides. The smallest active peptide has the sequence Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- His-Asp . This 20-amino-acid-residue peptide has 20-40% of the activity of the native molecule and a Ki of 0.2 nM. Inhibition, as a minimum, appears to be based upon the inhibitor protein containing the recognition sequences that dictate protein-substrate-specificity. This inhibitory peptide also has sequence homology with the phosphorylation site for a protein kinase other than the cyclic AMP-dependent enzyme.</jats:p>
Umfang:	655-661
ISSN:	0264-6021 1470-8728
DOI:	10.1042/bj2310655