2hwn: Difference between revisions
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'''Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide''' | {{Structure | ||
|PDB= 2hwn |SIZE=350|CAPTION= <scene name='initialview01'>2hwn</scene>, resolution 1.600Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</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] | |||
|GENE= Prkar2a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |||
}} | |||
'''Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HWN is a [ | 2HWN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HWN OCA]. | ||
==Reference== | ==Reference== | ||
A dynamic mechanism for AKAP binding to RII isoforms of cAMP-dependent protein kinase., Kinderman FS, Kim C, von Daake S, Ma Y, Pham BQ, Spraggon G, Xuong NH, Jennings PA, Taylor SS, Mol Cell. 2006 Nov 3;24(3):397-408. PMID:[http:// | A dynamic mechanism for AKAP binding to RII isoforms of cAMP-dependent protein kinase., Kinderman FS, Kim C, von Daake S, Ma Y, Pham BQ, Spraggon G, Xuong NH, Jennings PA, Taylor SS, Mol Cell. 2006 Nov 3;24(3):397-408. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17081990 17081990] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: regulatory subunit]] | [[Category: regulatory subunit]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:22:34 2008'' | ||
Revision as of 15:22, 20 March 2008
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| 2hwn, resolution 1.600Å | |||||||||||||
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| Ligands: | GOL | ||||||||||||
| Gene: | Prkar2a (Rattus norvegicus) | ||||||||||||
| Activity: | cAMP-dependent protein kinase, with EC number 2.7.11.11 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide
Overview
A kinase-anchoring proteins (AKAPs) target PKA to specific microdomains by using an amphipathic helix that docks to N-terminal dimerization and docking (D/D) domains of PKA regulatory (R) subunits. To understand specificity, we solved the crystal structure of the helical motif from D-AKAP2, a dual-specific AKAP, bound to the RIIalpha D/D domain. The 1.6 Angstrom structure reveals how this dynamic, hydrophobic docking site is assembled. A stable, hydrophobic docking groove is formed by the helical interface of two RIIalpha protomers. The flexible N terminus of one protomer is then recruited to the site, anchored to the peptide through two essential isoleucines. The other N terminus is disordered. This asymmetry provides greater possibilities for AKAP docking. Although there is strong discrimination against RIalpha in the N terminus of the AKAP helix, the hydrophobic groove discriminates against RIIalpha. RIalpha, with a cavity in the groove, can accept a bulky tryptophan, whereas RIIalpha requires valine.
About this Structure
2HWN is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
A dynamic mechanism for AKAP binding to RII isoforms of cAMP-dependent protein kinase., Kinderman FS, Kim C, von Daake S, Ma Y, Pham BQ, Spraggon G, Xuong NH, Jennings PA, Taylor SS, Mol Cell. 2006 Nov 3;24(3):397-408. PMID:17081990
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