2drn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2drn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2drn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2drn| PDB=2drn | SCENE= }}
{{STRUCTURE_2drn| PDB=2drn | SCENE= }}
-
'''Docking and dimerization domain (D/D) of the Type II-alpha regulatory subunity of protein kinase A (PKA) in complex with a peptide from an A-kinase anchoring protein'''
+
===Docking and dimerization domain (D/D) of the Type II-alpha regulatory subunity of protein kinase A (PKA) in complex with a peptide from an A-kinase anchoring protein===
-
==Overview==
+
<!--
-
The specificity of intracellular signaling events is controlled, in part, by compartmentalization of protein kinases and phosphatases. The subcellular localization of these enzymes is often maintained by protein- protein interactions. A prototypic example is the compartmentalization of the cAMP-dependent protein kinase (PKA) through its association with A-kinase anchoring proteins (AKAPs). A docking and dimerization domain (D/D) located within the first 45 residues of each regulatory (R) subunit protomer forms a high affinity binding site for its anchoring partner. We now report the structures of two D/D-AKAP peptide complexes obtained by solution NMR methods, one with Ht31(493-515) and the other with AKAP79(392-413). We present the first direct structural data demonstrating the helical nature of the peptides. The structures reveal conserved hydrophobic interaction surfaces on the helical AKAP peptides and the PKA R subunit, which are responsible for mediating the high affinity association in the complexes. In a departure from the dimer-dimer interactions seen in other X-type four-helix bundle dimeric proteins, our structures reveal a novel hydrophobic groove that accommodates one AKAP per RIIalpha D/D.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11285229}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11285229 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11285229}}
==About this Structure==
==About this Structure==
-
2DRN is a [[Protein complex]] structure of sequences 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=2DRN OCA].
+
2DRN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRN OCA].
==Reference==
==Reference==
Line 37: Line 41:
[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:00:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:49:41 2008''

Revision as of 10:49, 29 July 2008

Image:2drn.png

Template:STRUCTURE 2drn

Docking and dimerization domain (D/D) of the Type II-alpha regulatory subunity of protein kinase A (PKA) in complex with a peptide from an A-kinase anchoring protein

Template:ABSTRACT PUBMED 11285229

About this Structure

2DRN is a Protein complex structure of sequences from Rattus norvegicus. Full experimental information is available from OCA.

Reference

A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes., Newlon MG, Roy M, Morikis D, Carr DW, Westphal R, Scott JD, Jennings PA, EMBO J. 2001 Apr 2;20(7):1651-62. PMID:11285229

Page seeded by OCA on Tue Jul 29 13:49:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2drn"
Personal tools