Structural modeling of the catalytic subunit-regulatory subunit dimeric complex of the camp-dependent protein kinase.

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The cAMP-dependent protein kinase (PKA) is a multifunctional kinase that serves as a prototype for understanding second messenger signaling and protein phosphorylation. In the absence of a cAMP signal, PKA exists as a dimer of dimers, consisting of two regulatory (R) and two catalystic (C) subunits. Based on experimentally derived data (i.e., crystal structures of the R and C subunits, mutagenesis data identifying points of subunit-subunit contacts), the neutron scattering derived model for the heterodimer (Zhao et al., 1998) and using a set of computational approaches (homology modeling, Monte Carlo simulation), they have developed a high-resolution model of the RII{alpha}-C{alpha} ... continued below

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13 p.

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Tung, C-S (Chang-Shung); Gallagher, S. C. (Stephen C.); Walsh, D. A. (Donal A.) & Trewhella, J. (Jill) January 1, 2001.

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Description

The cAMP-dependent protein kinase (PKA) is a multifunctional kinase that serves as a prototype for understanding second messenger signaling and protein phosphorylation. In the absence of a cAMP signal, PKA exists as a dimer of dimers, consisting of two regulatory (R) and two catalystic (C) subunits. Based on experimentally derived data (i.e., crystal structures of the R and C subunits, mutagenesis data identifying points of subunit-subunit contacts), the neutron scattering derived model for the heterodimer (Zhao et al., 1998) and using a set of computational approaches (homology modeling, Monte Carlo simulation), they have developed a high-resolution model of the RII{alpha}-C{alpha} dimer. The nature of the subunit-subunit interface was studied. The model reveals an averaged size dimer interface (2100 Angstrom{sup 2}) that is distant from the pseudo-substrate binding site on the C subunit. The additional contacts made by the pseudosubstrate increases the stability of the dimeric complex. Based on a set of R-C dimer structures derived using a simulated annealing approach, specific interactions (hydrogen bonds) between the two subunits and were identified.

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13 p.

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  • "Submitted to: Biophysical Society Meeting, Boston, MA, Feb. 17-22, 2001"

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  • Report No.: LA-UR-01-0963
  • Report No.: LA-UR-01-963
  • Grant Number: none
  • Office of Scientific & Technical Information Report Number: 975141
  • Archival Resource Key: ark:/67531/metadc925595

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Reports, articles and other documents harvested from the Office of Scientific and Technical Information.

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  • January 1, 2001

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  • Nov. 13, 2016, 7:26 p.m.

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  • Dec. 12, 2016, 6:41 p.m.

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Tung, C-S (Chang-Shung); Gallagher, S. C. (Stephen C.); Walsh, D. A. (Donal A.) & Trewhella, J. (Jill). Structural modeling of the catalytic subunit-regulatory subunit dimeric complex of the camp-dependent protein kinase., article, January 1, 2001; United States. (digital.library.unt.edu/ark:/67531/metadc925595/: accessed April 22, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.