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2h9r

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[[Image:2h9r.gif|left|200px]]
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{{Seed}}
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[[Image:2h9r.png|left|200px]]
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{{STRUCTURE_2h9r| PDB=2h9r | SCENE= }}
{{STRUCTURE_2h9r| PDB=2h9r | SCENE= }}
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'''Docking and dimerization domain (D/D) of the regulatory subunit of the Type II-alpha cAMP-dependent protein kinase A associated with a Peptide derived from an A-kinase anchoring protein (AKAP)'''
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===Docking and dimerization domain (D/D) of the regulatory subunit of the Type II-alpha cAMP-dependent protein kinase A associated with a Peptide derived from an A-kinase anchoring protein (AKAP)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11285229 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11285229}}
==About this Structure==
==About this Structure==
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2H9R 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=2H9R OCA].
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2H9R 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=2H9R OCA].
==Reference==
==Reference==
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[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:01:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:52:07 2008''

Revision as of 07:52, 28 July 2008

Image:2h9r.png

Template:STRUCTURE 2h9r

Docking and dimerization domain (D/D) of the regulatory subunit of the Type II-alpha cAMP-dependent protein kinase A associated with a Peptide derived from an A-kinase anchoring protein (AKAP)

Template:ABSTRACT PUBMED 11285229

About this Structure

2H9R 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 Mon Jul 28 10:52:07 2008

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