2hwn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2hwn.gif|left|200px]]
[[Image:2hwn.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2hwn |SIZE=350|CAPTION= <scene name='initialview01'>2hwn</scene>, resolution 1.600&Aring;
+
The line below this paragraph, containing "STRUCTURE_2hwn", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|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>
+
or leave the SCENE parameter empty for the default display.
-
|GENE= Prkar2a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2hwn| PDB=2hwn | SCENE= }}
-
|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>
+
-
}}
+
'''Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide'''
'''Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide'''
Line 25: Line 22:
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: cAMP-dependent protein kinase]]
+
[[Category: CAMP-dependent protein kinase]]
[[Category: Kim, C.]]
[[Category: Kim, C.]]
[[Category: Kinderman, F.]]
[[Category: Kinderman, F.]]
-
[[Category: akap]]
+
[[Category: Akap]]
-
[[Category: d/d]]
+
[[Category: D/d]]
-
[[Category: dimerization/docking]]
+
[[Category: Dimerization/docking]]
-
[[Category: pka]]
+
[[Category: Pka]]
-
[[Category: regulatory subunit]]
+
[[Category: Regulatory subunit]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:48:10 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:36:31 2008''
+

Revision as of 03:48, 4 May 2008

Template:STRUCTURE 2hwn

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 Sun May 4 06:48:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools