2hwn
From Proteopedia
(New page: 200px<br /><applet load="2hwn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hwn, resolution 1.600Å" /> '''Crystal Structure o...) |
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| - | [[Image:2hwn.gif|left|200px]]<br /><applet load="2hwn" size=" | + | [[Image:2hwn.gif|left|200px]]<br /><applet load="2hwn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hwn, resolution 1.600Å" /> | caption="2hwn, resolution 1.600Å" /> | ||
'''Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide'''<br /> | '''Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A kinase-anchoring proteins (AKAPs) target PKA to specific microdomains by | + | 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== | ==About this Structure== | ||
| - | 2HWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 2HWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HWN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: regulatory subunit]] | [[Category: regulatory subunit]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:41 2008'' |
Revision as of 15:46, 21 February 2008
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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 with as ligand. Active as cAMP-dependent protein kinase, with EC number 2.7.11.11 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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