1NY3

Crystal structure of ADP bound to MAP KAP kinase 2

Summary for 1NY3

• Entry DOI: 10.2210/pdb1ny3/pdb
• Related: 1NXK
• Descriptor: MAP kinase-activated protein kinase 2, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: map kap kinase 2, mk2, adp, kinase, ser/thr kinase, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 46056.94

Authors

Underwood, K.W.,Parris, K.D.,Federico, E.,Mosyak, L.,Shane, T.,Taylor, M.,Svenson, K.,Liu, Y.,Hsiao, C.L.,Wolfrom, S.,Maguire, M.,Malakian, K.,Telliez, J.B.,Lin, L.L.,Kriz, R.W.,Seehra, J.,Somers, W.S.,Stahl, M.L. (deposition date: 2003-02-11, release date: 2003-10-14, Last modification date: 2023-08-16)

Primary citation

Underwood, K.W.,Parris, K.D.,Federico, E.,Mosyak, L.,Czerwinski, R.M.,Shane, T.,Taylor, M.,Svenson, K.,Liu, Y.,Hsiao, C.L.,Wolfrom, S.,Maguire, M.,Malakian, K.,Telliez, J.B.,Lin, L.L.,Kriz, R.W.,Seehra, J.,Somers, W.S.,Stahl, M.L.
Catalytically active MAP KAP kinase 2 structures in complex with staurosporine and ADP reveal differences with the autoinhibited enzyme
Structure, 11:627-636, 2003

PubMed Abstract: 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.

PubMed: 12791252
DOI: 10.1016/S0969-2126(03)00092-3

Experimental method

X-RAY DIFFRACTION (3 Å)