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2kdu

From Proteopedia

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[[Image:2kdu.png|left|200px]]
 
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==Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode==
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The line below this paragraph, containing "STRUCTURE_2kdu", creates the "Structure Box" on the page.
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<StructureSection load='2kdu' size='340' side='right'caption='[[2kdu]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2kdu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KDU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_2kdu| PDB=2kdu | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdu OCA], [https://pdbe.org/2kdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kdu RCSB], [https://www.ebi.ac.uk/pdbsum/2kdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/2kdu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2kdu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ca(2+) signalling in neurons through calmodulin (CaM) has a prominent function in regulating synaptic vesicle trafficking, transport, and fusion. Importantly, Ca(2+)-CaM binds a conserved region in the priming proteins Munc13-1 and ubMunc13-2 and thus regulates synaptic neurotransmitter release in neurons in response to residual Ca(2+) signals. We solved the structure of Ca(2+)(4)-CaM in complex with the CaM-binding domain of Munc13-1, which features a novel 1-5-8-26 CaM-binding motif with two separated mobile structural modules, each involving a CaM domain. Photoaffinity labelling data reveal the same modular architecture in the complex with the ubMunc13-2 isoform. The N-module can be dissociated with EGTA to form the half-loaded Munc13/Ca(2+)(2)-CaM complex. The Ca(2+) regulation of these Munc13 isoforms can therefore be explained by the modular nature of the Munc13/Ca(2+)-CaM interactions, where the C-module provides a high-affinity interaction activated at nanomolar [Ca(2+)](i), whereas the N-module acts as a sensor at micromolar [Ca(2+)](i). This Ca(2+)/CaM-binding mode of Munc13 likely constitutes a key molecular correlate of the characteristic Ca(2+)-dependent modulation of short-term synaptic plasticity.
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===Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode===
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Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity.,Rodriguez-Castaneda F, Maestre-Martinez M, Coudevylle N, Dimova K, Junge H, Lipstein N, Lee D, Becker S, Brose N, Jahn O, Carlomagno T, Griesinger C EMBO J. 2010 Feb 3;29(3):680-91. Epub 2009 Dec 10. PMID:20010694<ref>PMID:20010694</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20010694}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2kdu" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20010694 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20010694}}
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==About this Structure==
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[[2kdu]] is a 2 chain structure of [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDU OCA].
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==See Also==
==See Also==
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*[[Calmodulin]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:20010694</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Becker, S.]]
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[[Category: Becker S]]
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[[Category: Brose, N.]]
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[[Category: Brose N]]
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[[Category: Carlomagno, T.]]
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[[Category: Carlomagno T]]
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[[Category: Coudevylle, N.]]
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[[Category: Coudevylle N]]
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[[Category: Dimova, K.]]
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[[Category: Dimova K]]
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[[Category: Griesinger, C.]]
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[[Category: Griesinger C]]
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[[Category: Jahn, O.]]
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[[Category: Jahn O]]
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[[Category: Junge, H.]]
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[[Category: Junge H]]
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[[Category: Maestre-Martinez, M.]]
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[[Category: Maestre-Martinez M]]
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[[Category: Rodriguez-Castaneda, F A.]]
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[[Category: Rodriguez-Castaneda FA]]
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[[Category: Acetylation]]
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[[Category: Alternative splicing]]
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[[Category: Calcium]]
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[[Category: Calmodulin]]
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[[Category: Cell junction]]
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[[Category: Cell membrane]]
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[[Category: Coiled coil]]
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[[Category: Cytoplasm]]
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[[Category: Exocytosis]]
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[[Category: Membrane]]
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[[Category: Metal binding protein-exocytosis complex]]
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[[Category: Metal binding protein-protein binding complex]]
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[[Category: Metal-binding]]
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[[Category: Methylation]]
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[[Category: Munc13]]
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[[Category: Phorbol-ester binding]]
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[[Category: Phosphoprotein]]
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[[Category: Protein]]
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[[Category: Synapse]]
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[[Category: Zinc]]
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[[Category: Zinc-finger]]
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Current revision

Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode

PDB ID 2kdu

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