PDBsum entry: 2h9r

Transferase

PDB id: 2h9r

Contents

Protein chains

46 a.a. *

22 a.a. *

* Residue conservation analysis

PDB id:

2h9r

Name:

Transferase

Title:

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)

Structure:

Camp-dependent protein kinase type ii-alpha regulatory subunit. Chain: a, b. Fragment: n-terminal docking and dimerization domain, residues 4-46. Engineered: yes. 22-mer from a-kinase anchor protein 5. Chain: c. Fragment: pka-rii subunit binding domain.

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: riia(1-44). Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide has been generated by solid phase peptide synthesis.. This sequence occurs naturally

NMR struc:

10 models

Authors:

M.G.Newlon,M.Roy,D.Morikis,Z.E.Hausken,V.Coghlan,J.D.Scott, P.A.Jennings

Key ref:

M.G.Newlon et al. (2001). A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. EMBO J, 20, 1651-1662. PubMed id: 11285229 DOI: 10.1093/emboj/20.7.1651

Date:

10-Jun-06 Release date: 29-Aug-06

Protein chains

P12368  (KAP2_RAT) -  cAMP-dependent protein kinase type II-alpha regulatory subunit

Seq: 401 a.a.

Struc: 46 a.a.*

Protein chain

	No UniProt id for this chain
	* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biological process: signal transduction (1 term)
• Biochemical function: cAMP-dependent protein kinase regulator activity (1 term)

DOI no: 10.1093/emboj/20.7.1651

EMBO J 20:1651-1662 (2001)

PubMed id: 11285229

A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.

M.G.Newlon, M.Roy, D.Morikis, D.W.Carr, R.Westphal, J.D.Scott, P.A.Jennings.

ABSTRACT

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.

Selected figure(s)

Figure 5.
Figure 5 NOE contacts between RII and Ht31 and AKAP79. (A and B) The NOE contacts for each residue on the Ht31 (green) or AKAP79 (purple) to RII (A) or on RII to each of the AKAPs (B). (C and D) Structural view of the NOE contacts. RII is colored yellow and gray for each protomer. Ht31 (C) is colored green and AKAP79 (D) is colored purple. All of the residues that have observed NOE contacts are indicated.

Figure 7.
Figure 7 Schematic diagram of protein−protein interactions mediated by X-type four-helix bundles. RII is unique in binding one protomer per dimer at a surface hydrophobic groove. HNF-1 presents a hydrophobic face and forms a dimer of dimers. Likewise, the stoichiometry of P53 binding to S100 is two peptides per dimer. The binding interactions with SAM are under investigation.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2001, 20, 1651-1662) copyright 2001.

Figures were selected by the author.