PDBsum entry 3cik

Transferase/signaling protein

PDB id: 3cik

Contents

Protein chains

619 a.a. *

339 a.a. *

61 a.a. *

Metals

_MG

Waters ×19

* Residue conservation analysis

PDB id:

3cik

Name:

Transferase/signaling protein

Title:

Human grk2 in complex with gbetagamma subunits

Structure:

Beta-adrenergic receptor kinase 1. Chain: a. Synonym: beta-ark-1, g-protein coupled receptor kinase 2. Engineered: yes. Guanine nucleotide-binding protein g(i)/g(s)/g(t) subunit beta-1. Chain: b. Synonym: transducin beta chain 1. Engineered: yes.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: adrbk1, bark, bark1, grk2. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Bos taurus. Bovine. Organism_taxid: 9913.

Resolution:

2.75Å R-factor: 0.208 R-free: 0.269

Authors:

J.J.G.Tesmer,D.T.Lodowski

Key ref:

J.J.Tesmer et al. (2010). Structure of human G protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol. J Med Chem, 53, 1867-1870. PubMed id: 20128603

Date:

11-Mar-08 Release date: 17-Feb-09

Protein chain

P25098  (ARBK1_HUMAN) -  Beta-adrenergic receptor kinase 1 from Homo sapiens

Seq: 689 a.a.

Struc: 619 a.a.

Protein chain

P62871  (GBB1_BOVIN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 from Bos taurus

Seq: 340 a.a.

Struc: 339 a.a.

Protein chain

P63212  (GBG2_BOVIN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 from Bos taurus

Seq: 71 a.a.

Struc: 61 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chain A: E.C.2.7.11.15 - [beta-adrenergic-receptor] kinase.
• Reaction: [beta-adrenergic receptor] + ATP = [beta-adrenergic receptor]-phosphate + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Med Chem 53:1867-1870 (2010)

PubMed id: 20128603

Structure of human G protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol.

J.J.Tesmer, V.M.Tesmer, D.T.Lodowski, H.Steinhagen, J.Huber.

ABSTRACT

G protein-coupled receptor kinase 2 (GRK2) is a pharmaceutical target for the treatment of cardiovascular diseases such as congestive heart failure, myocardial infarction, and hypertension. To better understand how nanomolar inhibition and selectivity for GRK2 might be achieved, we have determined crystal structures of human GRK2 in complex with Gbetagamma in the presence and absence of the AGC kinase inhibitor balanol. The selectivity of balanol among human GRKs is assessed.