1hzm: Difference between revisions
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[[Image:1hzm.jpg|left|200px]] | [[Image:1hzm.jpg|left|200px]] | ||
'''STRUCTURE OF ERK2 BINDING DOMAIN OF MAPK PHOSPHATASE MKP-3: STRUCTURAL INSIGHTS INTO MKP-3 ACTIVATION BY ERK2''' | {{Structure | ||
|PDB= 1hzm |SIZE=350|CAPTION= <scene name='initialview01'>1hzm</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF ERK2 BINDING DOMAIN OF MAPK PHOSPHATASE MKP-3: STRUCTURAL INSIGHTS INTO MKP-3 ACTIVATION BY ERK2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HZM is a [ | 1HZM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZM OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2., Farooq A, Chaturvedi G, Mujtaba S, Plotnikova O, Zeng L, Dhalluin C, Ashton R, Zhou MM, Mol Cell. 2001 Feb;7(2):387-99. PMID:[http:// | Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2., Farooq A, Chaturvedi G, Mujtaba S, Plotnikova O, Zeng L, Dhalluin C, Ashton R, Zhou MM, Mol Cell. 2001 Feb;7(2):387-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11239467 11239467] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:34 2008'' | ||
Revision as of 09:43, 20 March 2008
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STRUCTURE OF ERK2 BINDING DOMAIN OF MAPK PHOSPHATASE MKP-3: STRUCTURAL INSIGHTS INTO MKP-3 ACTIVATION BY ERK2
Overview
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.
About this Structure
1HZM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2., Farooq A, Chaturvedi G, Mujtaba S, Plotnikova O, Zeng L, Dhalluin C, Ashton R, Zhou MM, Mol Cell. 2001 Feb;7(2):387-99. PMID:11239467
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