1ny3

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spinqualitylabelsall models 1ny3, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of ADP bound to MAP KAP kinase 2

Overview

MAP KAP kinase 2 (MK2), a Ser/Thr kinase, plays a crucial role in the, inflammatory process. We have determined the crystal structures of a, catalytically active C-terminal deletion form of human MK2, residues, 41-364, in complex with staurosporine at 2.7 A and with ADP at 3.2 A, revealing overall structural similarity with other Ser/Thr kinases., Kinetic analysis reveals that the K(m) for ATP is very similar for MK2, 41-364 and p38-activated MK2 41-400. Conversely, the catalytic rate and, binding for peptide substrate are dramatically reduced in MK2 41-364., However, phosphorylation of MK2 41-364 by p38 restores the V(max) and K(m), for peptide substrate to values comparable to those seen in p38-activated, MK2 41-400, suggesting a mechanism for regulation of enzyme activity.

About this Structure

1NY3 is a Single protein structure of sequence from Homo sapiens with ADP as ligand. Full crystallographic information is available from OCA.

Reference

Catalytically active MAP KAP kinase 2 structures in complex with staurosporine and ADP reveal differences with the autoinhibited enzyme., Underwood KW, Parris KD, Federico E, Mosyak L, Czerwinski RM, Shane T, Taylor M, Svenson K, Liu Y, Hsiao CL, Wolfrom S, Maguire M, Malakian K, Telliez JB, Lin LL, Kriz RW, Seehra J, Somers WS, Stahl ML, Structure. 2003 Jun;11(6):627-36. PMID:12791252

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