1hzm: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1hzm.gif|left|200px]]<br />
-<applet load="1hzm" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1hzm" />
-'''STRUCTURE OF ERK2 BINDING DOMAIN OF MAPK PHOSPHATASE MKP-3: STRUCTURAL INSIGHTS INTO MKP-3 ACTIVATION BY ERK2'''<br />
-==Overview==
+==STRUCTURE OF ERK2 BINDING DOMAIN OF MAPK PHOSPHATASE MKP-3: STRUCTURAL INSIGHTS INTO MKP-3 ACTIVATION BY ERK2==
-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.
+<StructureSection load='1hzm' size='340' side='right'caption='[[1hzm]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hzm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZM FirstGlance]. <br>
+</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=1hzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzm OCA], [https://pdbe.org/1hzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzm RCSB], [https://www.ebi.ac.uk/pdbsum/1hzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DUS6_HUMAN DUS6_HUMAN] Inactivates MAP kinases. Has a specificity for the ERK family.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/1hzm_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1hzm ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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<ref>PMID:11239467</ref>
-HZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HZM OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11239467 11239467]
+</div>
+<div class="pdbe-citations 1hzm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[MAP kinase phosphatase|MAP kinase phosphatase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Farooq, A.]]
+[[Category: Farooq A]]
-[[Category: Zhou, M.M.]]
+[[Category: Zhou M-M]]
-[[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:24:40 2007''