1u5r

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models PDB ID 1u5r Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.1Å
Ligands:	, and
Gene:	serine/threonine protein kinase TAO2 (Rattus norvegicus)
Coordinates:	save as pdb, mmCIF, xml

Crystal Structure of the TAO2 Kinase Domain: Activation and Specifity of a Ste20p MAP3K

Overview

TAO2 is a mitogen-activated protein kinase kinase kinase (MAP3K) that doubly phosphorylates and activates the MAP kinase kinases (MAP2Ks) MEK3 and MEK6. The structure of the kinase domain of TAO2 (1-320) has been solved in its phosphorylated active conformation. The structure, together with structure-based mutagenic analysis, reveals that positively charged residues in the substrate binding groove mediate the first step in the dual phosphorylation of MEK6, on the threonine residue in the motif DS*VAKT*I (*denotes phosphorylation site) of MEK6. TAO2 is a Ste20p homolog, and the structure of active TAO2, in comparison with that of low-activity p21-activated protein kinase (PAK1), a Ste20p-related MAP4K, reveals how this group of kinases is activated by phosphorylation. Finally, active TAO2 displays unusual interactions with ATP, involving, in part, a subgroup-specific C-terminal extension of TAO2. The observed interactions may be useful in making specific inhibitors of TAO kinases.

About this Structure

1U5R is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K., Zhou T, Raman M, Gao Y, Earnest S, Chen Z, Machius M, Cobb MH, Goldsmith EJ, Structure. 2004 Oct;12(10):1891-900. PMID:15458637

Page seeded by OCA on Thu Mar 20 14:27:36 2008