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Literature DB >> 16625363

Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation.

Abstract

Using small-angle solution scattering and neutron contrast variation, we have studied the structure of the multi-subunit protein kinase A. We have gained insights into how nature can take a set of common structural domains (or themes) and modulate their interactions via sequence variations and second messenger mediated signaling to affect enzyme activity and receptor binding important for targeting this multi-function enzyme to specific sub-cellular locations. These studies demonstrate the power of neutron contrast variation to expand our knowledge of the dynamic supra-molecular structures that carry out biological function.

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Year: 2006 PMID： 16625363 DOI： 10.1007/s00249-006-0061-y

Source DB: PubMed Journal: Eur Biophys J ISSN： 0175-7571 Impact factor: 1.733

25 in total

1. A structural model of the catalytic subunit-regulatory subunit dimeric complex of the cAMP-dependent protein kinase.

Authors: Chang-Shung Tung; Donal A Walsh; Jill Trewhella
Journal: J Biol Chem Date: 2002-01-17 Impact factor: 5.157

Review 2. The essential role of RI alpha in the maintenance of regulated PKA activity.

Authors: Paul S Amieux; G Stanley McKnight
Journal: Ann N Y Acad Sci Date: 2002-06 Impact factor: 5.691

3. Related protein-protein interaction modules present drastically different surface topographies despite a conserved helical platform.

Authors: Poopak Banky; Melinda Roy; Marceen G Newlon; Dimitrios Morikis; Nina M Haste; Susan S Taylor; Patricia A Jennings
Journal: J Mol Biol Date: 2003-07-25 Impact factor: 5.469

4. Differential effects of substrate on type I and type II PKA holoenzyme dissociation.

Authors: Dominico Vigil; Donald K Blumenthal; Simon Brown; Susan S Taylor; Jill Trewhella
Journal: Biochemistry Date: 2004-05-18 Impact factor: 3.162

5. Reduced ocular dominance plasticity and long-term potentiation in the developing visual cortex of protein kinase A RII alpha mutant mice.

Authors: Yan Rao; Quentin S Fischer; Yupeng Yang; G Stanley McKnight; Adrienne LaRue; Nigel W Daw
Journal: Eur J Neurosci Date: 2004-08 Impact factor: 3.386

6. C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change.

Authors: William T Heller; Dominico Vigil; Simon Brown; Donald K Blumenthal; Susan S Taylor; Jill Trewhella
Journal: J Biol Chem Date: 2004-02-25 Impact factor: 5.157

Review 7. Substrate diversity of the cAMP-dependent protein kinase: regulation based upon multiple binding interactions.

Authors: D A Walsh; D B Glass; R D Mitchell
Journal: Curr Opin Cell Biol Date: 1992-04 Impact factor: 8.382

8. The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.

Authors: Dominico Vigil; Donald K Blumenthal; Susan S Taylor; Jill Trewhella
Journal: J Biol Chem Date: 2005-08-17 Impact factor: 5.157

Structural themes and variations in protein kinase A as seen by small-angle scattering and neutron contrast variation.

1. A structural model of the catalytic subunit-regulatory subunit dimeric complex of the cAMP-dependent protein kinase.

Review 2. The essential role of RI alpha in the maintenance of regulated PKA activity.

3. Related protein-protein interaction modules present drastically different surface topographies despite a conserved helical platform.

4. Differential effects of substrate on type I and type II PKA holoenzyme dissociation.

5. Reduced ocular dominance plasticity and long-term potentiation in the developing visual cortex of protein kinase A RII alpha mutant mice.

6. C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change.

Review 7. Substrate diversity of the cAMP-dependent protein kinase: regulation based upon multiple binding interactions.

8. The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.

Review 9. Insights into biomolecular function from small-angle scattering.

10. The molecular basis for protein kinase A anchoring revealed by solution NMR.

1. The amino terminus of cGMP-dependent protein kinase Iβ increases the dynamics of the protein's cGMP-binding pockets.

2. Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1.