This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 23: | Line 23: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 17:46:41 2008
