1m3g: Difference between revisions

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New page: left|200px<br /> <applet load="1m3g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3g" /> '''SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN ...
 
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[[Image:1m3g.gif|left|200px]]<br />
[[Image:1m3g.gif|left|200px]]<br /><applet load="1m3g" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1m3g" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1m3g" />
caption="1m3g" />
'''SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION'''<br />
'''SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION'''<br />


==Overview==
==Overview==
Inactivation of mitogen-activated protein kinases (MAPKs) by MAPK, phosphatases (MKPs) is accomplished via substrate-induced activation of, the latter enzymes; however, the structural basis for the underlying, mechanism remains elusive. Here, we report the three-dimensional solution, structure of the C-terminal phosphatase domain of the prototypical MKP, PAC-1, determined when bound to phosphate. Structural and biochemical, analyses reveal unique active site geometry of the enzyme important for, binding to phosphorylated threonine and tyrosine of MAPK ERK2. Our study, further demonstrates that the dynamic interaction between the N-terminal, kinase binding domain and the C-terminal phosphatase domain of an MKP is, directly coupled to MAPK-induced conformational change of the phosphatase, active site, which is essential for eliciting its full enzymatic activity.
Inactivation of mitogen-activated protein kinases (MAPKs) by MAPK phosphatases (MKPs) is accomplished via substrate-induced activation of the latter enzymes; however, the structural basis for the underlying mechanism remains elusive. Here, we report the three-dimensional solution structure of the C-terminal phosphatase domain of the prototypical MKP PAC-1, determined when bound to phosphate. Structural and biochemical analyses reveal unique active site geometry of the enzyme important for binding to phosphorylated threonine and tyrosine of MAPK ERK2. Our study further demonstrates that the dynamic interaction between the N-terminal kinase binding domain and the C-terminal phosphatase domain of an MKP is directly coupled to MAPK-induced conformational change of the phosphatase active site, which is essential for eliciting its full enzymatic activity.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1M3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 1IKZ. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M3G OCA].  
1M3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1IKZ. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3G OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Farooq, A.]]
[[Category: Farooq, A.]]
[[Category: Zhou, M.M.]]
[[Category: Zhou, M M.]]
[[Category: catalytic domain]]
[[Category: catalytic domain]]
[[Category: mapk phosphatase]]
[[Category: mapk phosphatase]]
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[[Category: pac-1]]
[[Category: pac-1]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:06:43 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:03 2008''