2izx: Difference between revisions
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|PDB= 2izx |SIZE=350|CAPTION= <scene name='initialview01'>2izx</scene>, resolution 1.30Å | |PDB= 2izx |SIZE=350|CAPTION= <scene name='initialview01'>2izx</scene>, resolution 1.30Å | ||
|SITE= <scene name='pdbsite=AC1:Dtd+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Dtd+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=DTD:DITHIANE DIOL'>DTD</scene> | |LIGAND= <scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2izx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izx OCA], [http://www.ebi.ac.uk/pdbsum/2izx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2izx RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Localization of cyclic AMP (cAMP)-dependent protein kinase (PKA) by A kinase-anchoring proteins (AKAPs) restricts the action of this broad specificity kinase. The high-resolution crystal structures of the docking and dimerization (D/D) domain of the RIIalpha regulatory subunit of PKA both in the apo state and in complex with the high-affinity anchoring peptide AKAP-IS explain the molecular basis for AKAP-regulatory subunit recognition. AKAP-IS folds into an amphipathic alpha helix that engages an essentially preformed shallow groove on the surface of the RII dimer D/D domains. Conserved AKAP aliphatic residues dominate interactions to RII at the predominantly hydrophobic interface, whereas polar residues are important in conferring R subunit isoform specificity. Using a peptide screening approach, we have developed SuperAKAP-IS, a peptide that is 10,000-fold more selective for the RII isoform relative to RI and can be used to assess the impact of PKA isoform-selective anchoring on cAMP-responsive events inside cells. | Localization of cyclic AMP (cAMP)-dependent protein kinase (PKA) by A kinase-anchoring proteins (AKAPs) restricts the action of this broad specificity kinase. The high-resolution crystal structures of the docking and dimerization (D/D) domain of the RIIalpha regulatory subunit of PKA both in the apo state and in complex with the high-affinity anchoring peptide AKAP-IS explain the molecular basis for AKAP-regulatory subunit recognition. AKAP-IS folds into an amphipathic alpha helix that engages an essentially preformed shallow groove on the surface of the RII dimer D/D domains. Conserved AKAP aliphatic residues dominate interactions to RII at the predominantly hydrophobic interface, whereas polar residues are important in conferring R subunit isoform specificity. Using a peptide screening approach, we have developed SuperAKAP-IS, a peptide that is 10,000-fold more selective for the RII isoform relative to RI and can be used to assess the impact of PKA isoform-selective anchoring on cAMP-responsive events inside cells. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Scott, J D.]] | [[Category: Scott, J D.]] | ||
[[Category: Tasken, K.]] | [[Category: Tasken, K.]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: akap]] | [[Category: akap]] | ||
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[[Category: pka]] | [[Category: pka]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:51:05 2008'' | ||