1r2a

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[[Image:1r2a.gif|left|200px]]
[[Image:1r2a.gif|left|200px]]
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{{Structure
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|PDB= 1r2a |SIZE=350|CAPTION= <scene name='initialview01'>1r2a</scene>
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The line below this paragraph, containing "STRUCTURE_1r2a", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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|GENE= RIIA(1-44) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_1r2a| PDB=1r2a | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2a OCA], [http://www.ebi.ac.uk/pdbsum/1r2a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r2a RCSB]</span>
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'''THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR'''
'''THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR'''
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[[Category: Roy, M.]]
[[Category: Roy, M.]]
[[Category: Scott, J D.]]
[[Category: Scott, J D.]]
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[[Category: anchoring]]
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[[Category: Anchoring]]
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[[Category: four-helix bundle]]
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[[Category: Four-helix bundle]]
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[[Category: regulatory subunit]]
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[[Category: Regulatory subunit]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:59:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:22:13 2008''
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Revision as of 03:59, 3 May 2008

Image:1r2a.gif

Template:STRUCTURE 1r2a

THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR


Overview

Compartmentalization of signal transduction enzymes into signaling complexes is an important mechanism to ensure the specificity of intracellular events. Formation of these complexes is mediated by specialized protein motifs that participate in protein-protein interactions. The adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) is localized through interaction of the regulatory (R) subunit dimer with A-kinase-anchoring proteins (AKAPs). We now report the solution structure of the type II PKA R-subunit fragment RIIalpha(1-44), which encompasses both the AKAP-binding and dimerization interfaces. This structure incorporates an X-type four-helix bundle dimerization motif with an extended hydrophobic face that is necessary for high-affinity AKAP binding. NMR data on the complex between RIIalpha(1-44) and an AKAP fragment reveals extensive contacts between the two proteins. Interestingly, this same dimerization motif is present in other signaling molecules, the S100 family. Therefore, the X-type four-helix bundle may represent a conserved fold for protein-protein interactions in signal transduction.

About this Structure

1R2A is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The molecular basis for protein kinase A anchoring revealed by solution NMR., Newlon MG, Roy M, Morikis D, Hausken ZE, Coghlan V, Scott JD, Jennings PA, Nat Struct Biol. 1999 Mar;6(3):222-7. PMID:10074940 Page seeded by OCA on Sat May 3 06:59:16 2008

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