2acx
From Proteopedia
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Crystal Structure of G protein coupled receptor kinase 6 bound to AMPPNP
Overview
We describe the 2.6-A crystal structure of human G protein-coupled receptor kinase (GRK)-6, a key regulator of dopaminergic signaling and lymphocyte chemotaxis. GRK6 is a member of the GRK4 subfamily of GRKs, which is represented in most, if not all, metazoans. Comparison of GRK6 with GRK2 confirms that the catalytic core of all GRKs consists of intimately associated kinase and regulator of G protein signaling (RGS) homology domains. Despite being in complex with an ATP analog, the kinase domain of GRK6 remains in an open, presumably inactive conformation, suggesting that G protein-coupled receptors activate GRKs by inducing kinase domain closure. The structure reveals a putative phospholipid-binding site near the N terminus of GRK6 and structural elements within the kinase substrate channel that likely influence G protein-coupled receptor access and specificity. The crystalline GRK6 RGS homology domain forms an extensive dimer interface using conserved hydrophobic residues distinct from those in GRK2 that bind Galpha(q), although dimerization does not appear to occur in solution and is not required for receptor phosphorylation.
About this Structure
2ACX is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of G protein-coupled receptor kinase (GRK)-6 defines a second lineage of GRKs., Lodowski DT, Tesmer VM, Benovic JL, Tesmer JJ, J Biol Chem. 2006 Jun 16;281(24):16785-93. Epub 2006 Apr 13. PMID:16613860
Page seeded by OCA on Thu Feb 21 16:26:05 2008
Categories: Homo sapiens | Single protein | Benovic, J L. | Lodowski, D T. | Tesmer, J J. | Tesmer, V M. | ANP | MG | PO4 | G protein | G protein coupled receptor kinase | Grk | Grk6 | Kinase
