2izx

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|PDB= 2izx |SIZE=350|CAPTION= <scene name='initialview01'>2izx</scene>, resolution 1.30&Aring;
|PDB= 2izx |SIZE=350|CAPTION= <scene name='initialview01'>2izx</scene>, resolution 1.30&Aring;
|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>
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|LIGAND= <scene name='pdbligand=DTD:DITHIANE DIOL'>DTD</scene>
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|LIGAND= <scene name='pdbligand=DTD:DITHIANE+DIOL'>DTD</scene>
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|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]
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|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=
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|DOMAIN=
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|RELATEDENTRY=
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|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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}}
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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.
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==Disease==
 
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Known disease associated with this structure: Kallmann syndrome 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607123 607123]]
 
==About this Structure==
==About this Structure==
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[[Category: Scott, J D.]]
[[Category: Scott, J D.]]
[[Category: Tasken, K.]]
[[Category: Tasken, K.]]
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[[Category: DTD]]
 
[[Category: acetylation]]
[[Category: acetylation]]
[[Category: akap]]
[[Category: akap]]
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[[Category: pka]]
[[Category: pka]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:51:05 2008''

Revision as of 00:51, 31 March 2008

Image:2izx.jpg


PDB ID 2izx

Drag the structure with the mouse to rotate
, resolution 1.30Å
Sites:
Ligands:
Activity: cAMP-dependent protein kinase, with EC number 2.7.11.11
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



MOLECULAR BASIS OF AKAP SPECIFICITY FOR PKA REGULATORY SUBUNITS


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.

About this Structure

2IZX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular basis of AKAP specificity for PKA regulatory subunits., Gold MG, Lygren B, Dokurno P, Hoshi N, McConnachie G, Tasken K, Carlson CR, Scott JD, Barford D, Mol Cell. 2006 Nov 3;24(3):383-95. PMID:17081989

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