2hwn
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |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] | + | |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= Prkar2a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= Prkar2a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1r2a|1R2A]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hwn OCA], [http://www.ebi.ac.uk/pdbsum/2hwn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hwn RCSB]</span> | ||
}} | }} | ||
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[[Category: Kim, C.]] | [[Category: Kim, C.]] | ||
[[Category: Kinderman, F.]] | [[Category: Kinderman, F.]] | ||
| - | [[Category: GOL]] | ||
[[Category: akap]] | [[Category: akap]] | ||
[[Category: d/d]] | [[Category: d/d]] | ||
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[[Category: regulatory subunit]] | [[Category: regulatory subunit]] | ||
| - | ''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 03:36:31 2008'' |
Revision as of 00:36, 31 March 2008
| |||||||
| , resolution 1.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Prkar2a (Rattus norvegicus) | ||||||
| Activity: | cAMP-dependent protein kinase, with EC number 2.7.11.11 | ||||||
| Related: | 1R2A
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 03:36:31 2008
