2kn2: Difference between revisions

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-{{Seed}}
-[[Image:2kn2.png|left|200px]]
-<!--
+==Solution structure of the C-terminal domain of soybean calmodulin isoform 4 fused with the calmodulin-binding domain of NtMKP1==
-The line below this paragraph, containing "STRUCTURE_2kn2", creates the "Structure Box" on the page.
+<StructureSection load='2kn2' size='340' side='right'caption='[[2kn2]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2kn2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KN2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-{{STRUCTURE_2kn2|  PDB=2kn2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kn2 OCA], [https://pdbe.org/2kn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kn2 RCSB], [https://www.ebi.ac.uk/pdbsum/2kn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kn2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q39890_SOYBN Q39890_SOYBN]
+== 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/kn/2kn2_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=2kn2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The calcium regulatory protein calmodulin (CaM) binds in a calcium-dependent manner to numerous target proteins. The calmodulin-binding domain (CaMBD) region of Nicotiana tabacum MAPK phosphatase has an amino acid sequence that does not resemble the CaMBD of any other known Ca(2+)-CaM-binding proteins. Using a unique fusion protein strategy, we have been able to obtain a high resolution solution structure of the complex of soybean Ca(2+)-CaM4 (SCaM4) and this CaMBD. Complete isotope labeling of both parts of the complex in the fusion protein greatly facilitated the structure determination by NMR. The 12-residue CaMBD region was found to bind exclusively to the C-lobe of SCaM4. A specific Trp and Leu side chain are utilized to facilitate strong binding through a novel "double anchor" motif. Moreover, the orientation of the helical peptide on the surface of Ca(2+)-SCaM4 is distinct from other known complexes. The N-lobe of Ca(2+)-SCaM4 in the complex remains free for additional interactions and could possibly act as a calcium-dependent adapter protein. Signaling through the MAPK pathway and increases in intracellular Ca(2+) are both hallmarks of the plant stress response, and our data support the notion that coordination of these responses may occur through the formation of a unique CaM-MAPK phosphatase multiprotein complex.
-===Solution structure of the C-terminal domain of soybean calmodulin isoform 4 fused with the calmodulin-binding domain of NtMKP1===
+Structural studies of soybean calmodulin isoform 4 bound to the calmodulin-binding domain of tobacco mitogen-activated protein kinase phosphatase-1 provide insights into a sequential target binding mode.,Ishida H, Rainaldi M, Vogel HJ J Biol Chem. 2009 Oct 9;284(41):28292-305. Epub 2009 Aug 10. PMID:19667066<ref>PMID:19667066</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2kn2" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19667066}}, adds the Publication Abstract to the page
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19667066 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19667066}}
+__TOC__
+</StructureSection>
-==About this Structure==
-KN2 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KN2 OCA].
-==Reference==
-<ref group="xtra">PMID:19667066</ref><references group="xtra"/>
 [[Category: Glycine max]]
-[[Category: Ishida, H.]]
+[[Category: Large Structures]]
-[[Category: Rainaldi, M.]]
+[[Category: Ishida H]]
-[[Category: Vogel, H J.]]
+[[Category: Rainaldi M]]
-[[Category: Calmodulin]]
+[[Category: Vogel HJ]]
-[[Category: Calmodulin-target complex]]
-[[Category: Mapk phosphatase 1]]
-[[Category: Metal binding protein]]
-[[Category: Ntmkp1]]
-[[Category: Scam4]]
-[[Category: Soybean calmodulin]]
-[[Category: Tobacco mkp1]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 18 11:08:32 2010''