Molecular basis of the allosteric mechanism of cAMP in the regulatory PKA subunit.

Journal article

The second messenger cyclic Adenosine MonoPosphate (cAMP) mediates many biological process by interacting with structurally conserved nucleotide binding domains (cNBD's). Here, we use molecular dynamics simulations on RIIbeta-PKA, one of the best characterized members of the cNBD family, in presence and absence of cAMP. The results of our calculations are fully consistent with the available experimental data and suggest that the key factor of the cAMP allosteric mechanism in cNBDS's is the in...

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Authors: Pantano, S; Zaccolo, M; Carloni, P

• Journal: FEBS letters
• Volume: 579
• Issue: 12
• Pages: 2679-2685
• Publication date: 2005-05-01
• DOI: 10.1016/j.febslet.2005.02.084
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Computer Simulation; Cyclic AMP; Binding Sites; Protein Binding; Ligands; Protein Structure, Secondary; Protein Structure, Tertiary; Cyclic AMP-Dependent Protein Kinases; Crystallography, X-Ray; Water; Hydrogen Bonding; Gene Deletion; Sodium; X-Ray Diffraction; Protein Conformation; Protein Isoforms; Kinetics; Models, Molecular; Allosteric Regulation