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Science 26 July 1991:
Vol. 253. no. 5018, pp. 414 - 420
DOI: 10.1126/science.1862343
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Articles

Science, Vol 253, Issue 5018, 414-420
Copyright © 1991 by American Association for the Advancement of Science

articles

Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

DR Knighton, JH Zheng, LF Ten Eyck, NH Xuong, SS Taylor, and JM Sowadski

Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.

The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal structure of the complex is the basis of the analysis. The peptide inhibitor, derived from a naturally occurring heat-stable protein kinase inhibitor, contains an amphipathic helix that is followed by a turn and an extended conformation. The extended region occupies the cleft between the two lobes of the enzyme and contains a five-residue consensus recognition sequence common to all substrates and peptide inhibitors of the catalytic subunit. The helical portion of the peptide binds to a hydrophobic groove and conveys high affinity binding. Loops from both domains converge at the active site and contribute to a network of conserved residues at the sites of magnesium adenosine triphosphate binding and catalysis. Amino acids associated with peptide recognition, nonconserved, extend over a large surface area.


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J. Biol. Chem. 272, 916-923
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Identification of Critical Determinants for Autoinhibition in the Pseudosubstrate Region of Type Ialpha cAMP-dependent Protein Kinase.
C. E. Poteet-Smith, J. B. Shabb, S. H. Francis, and J. D. Corbin (1997)
J. Biol. Chem. 272, 379-388
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Oncogenic mutation in the Kit receptor tyrosine kinase alters substrate specificity and induces degradation of the protein tyrosine phosphatase SHP-1.
X. Piao, R. Paulson, P. van der Geer, T. Pawson, and A. Bernstein (1996)
PNAS 93, 14665-14669
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A positive genetic selection for disrupting protein-protein interactions: Identification of CREB mutations that prevent association with