1m3g

<StructureSection load='1m3g' size='340' side='right'caption='[[1m3g]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<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>

</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>

[[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.

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== 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>

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== References ==

<references/>

[[Category: Human]]

[[Category: Farooq, A]]

[[Category: Zhou, M M]]

[[Category: Pac-1]]