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==SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION==
==SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION==
<StructureSection load='1m3g' size='340' side='right'caption='[[1m3g]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1m3g' size='340' side='right'caption='[[1m3g]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1m3g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ikz 1ikz]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M3G FirstGlance]. <br>
<table><tr><td colspan='2'>[[1m3g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ikz 1ikz]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M3G FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m3g OCA], [https://pdbe.org/1m3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m3g RCSB], [https://www.ebi.ac.uk/pdbsum/1m3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m3g ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m3g OCA], [https://pdbe.org/1m3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m3g RCSB], [https://www.ebi.ac.uk/pdbsum/1m3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m3g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DUS2_HUMAN DUS2_HUMAN]] Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.  
[https://www.uniprot.org/uniprot/DUS2_HUMAN DUS2_HUMAN] Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m3g ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m3g ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP.,Farooq A, Plotnikova O, Chaturvedi G, Yan S, Zeng L, Zhang Q, Zhou MM Structure. 2003 Feb;11(2):155-64. PMID:12575935<ref>PMID:12575935</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1m3g" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[MAP kinase phosphatase|MAP kinase phosphatase]]
*[[MAP kinase phosphatase|MAP kinase phosphatase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Farooq, A]]
[[Category: Farooq A]]
[[Category: Zhou, M M]]
[[Category: Zhou M-M]]
[[Category: Catalytic domain]]
[[Category: Hydrolase]]
[[Category: Mapk phosphatase]]
[[Category: Pac-1]]

Revision as of 08:31, 10 April 2024

SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION

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