1HZM

STRUCTURE OF ERK2 BINDING DOMAIN OF MAPK PHOSPHATASE MKP-3: STRUCTURAL INSIGHTS INTO MKP-3 ACTIVATION BY ERK2

Summary for 1HZM

• Entry DOI: 10.2210/pdb1hzm/pdb
• Descriptor: DUAL SPECIFICITY PROTEIN PHOSPHATASE 6 (1 entity in total)
• Functional Keywords: hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q16828
• Total number of polymer chains: 1
• Total formula weight: 17424.75

Authors

Farooq, A.,Zhou, M.-M. (deposition date: 2001-01-25, release date: 2002-01-25, Last modification date: 2024-05-22)

Primary citation

Farooq, A.,Chaturvedi, G.,Mujtaba, S.,Plotnikova, O.,Zeng, L.,Dhalluin, C.,Ashton, R.,Zhou, M.M.
Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2.
Mol.Cell, 7:387-399, 2001

PubMed Abstract: MAP kinases (MAPKs), which control mitogenic signal transduction in all eukaryotic organisms, are inactivated by dual specificity MAPK phosphatases (MKPs). MKP-3, a prototypical MKP, achieves substrate specificity through its N-terminal domain binding to the MAPK ERK2, resulting in the activation of its C-terminal phosphatase domain. The solution structure and biochemical analysis of the ERK2 binding (EB) domain of MKP-3 show that regions that are essential for ERK2 binding partly overlap with its sites that interact with the C-terminal catalytic domain, and that these interactions are functionally coupled to the active site residues of MKP-3. Our findings suggest a novel mechanism by which the EB domain binding to ERK2 is transduced to cause a conformational change of the C-terminal catalytic domain, resulting in the enzymatic activation of MKP-3.

PubMed: 11239467
DOI: 10.1016/S1097-2765(01)00186-1

Experimental method

SOLUTION NMR