Structural modeling of the catalytic subunit-regulatory subunit dimeric complex of the camp-dependent protein kinase. [electronic resource]
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| Online Access: |
Online Access |
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| Corporate Author: | |
| Format: | Government Document Electronic eBook |
| Language: | English |
| Published: |
Washington, D.C. : Oak Ridge, Tenn. :
United States. Department of Energy ; distributed by the Office of Scientific and Technical Information, U.S. Department of Energy,
2001.
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| Subjects: |
| Abstract: | 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 RIIα-Cα dimer. The nature of the subunit-subunit interface was studied. The model reveals an averaged size dimer interface (2100 Angstrom²) 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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| Item Description: | Published through SciTech Connect. 01/01/2001. "la-ur-01-0963" " la-ur-01-963" "Submitted to: Biophysical Society Meeting, Boston, MA, Feb. 17-22, 2001" Trewhella, J.; Gallagher, S. C.; Tung, C-S; Walsh, D. A. |
| Physical Description: | 13 p. : digital, PDF file. |