1cff

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[[Image:1cff.png|left|200px]]
 
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==NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP==
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The line below this paragraph, containing "STRUCTURE_1cff", creates the "Structure Box" on the page.
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<StructureSection load='1cff' size='340' side='right'caption='[[1cff]]' 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'>[[1cff]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1CFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFF 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_1cff| PDB=1cff | 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=1cff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cff OCA], [https://pdbe.org/1cff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cff RCSB], [https://www.ebi.ac.uk/pdbsum/1cff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cff 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/cf/1cff_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=1cff 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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The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the plasma membrane calcium pump, the peptide C20W, has been solved by heteronuclear three-dimensional nuclear magnetic resonance (NMR) spectroscopy. The structure calculation is based on a total of 1808 intramolecular NOEs and 49 intermolecular NOEs between the peptide C20W and calmodulin from heteronuclear-filtered NOESY spectra and a half-filtered experiment, respectively. Chemical shift differences between free Ca(2+)-saturated CaM and its complex with C20W as well as the structure calculation reveal that C20W binds solely to the C-terminal half of CaM. In addition, comparison of the methyl resonances of the nine assigned methionine residues of free Ca(2+)-saturated CaM with those of the CaM/C20W complex revealed a significant difference between the N-terminal and the C-terminal domain; i.e., resonances in the N-terminal domain of the complex were much more similar to those reported for free CaM in contrast to those in the C-terminal half which were significantly different not only from the resonances of free CaM but also from those reported for the CaM/M13 complex. As a consequence, the global structure of the CaM/C20W complex is unusual, i.e., different from other peptide calmodulin complexes, since we find no indication for a collapsed structure. The fine modulation in the peptide protein interface shows a number of differences to the CaM/M13 complex studied by Ikura et al. [Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. (1992) Science 256, 632-638]. The unusual binding mode to only the C-terminal half of CaM is in agreement with the biochemical observation that the calcium pump can be activated by the C-terminal half of CaM alone [Guerini, D., Krebs, J., and Carafoli, E. (1984) J. Biol. Chem. 259, 15172-15177].
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===NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP===
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NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.,Elshorst B, Hennig M, Forsterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E Biochemistry. 1999 Sep 21;38(38):12320-32. PMID:10493800<ref>PMID:10493800</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_10493800}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1cff" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10493800 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10493800}}
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==About this Structure==
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[[1cff]] is a 2 chain structure of [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFF 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:10493800</ref><references group="xtra"/>
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__TOC__
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[[Category: Calcium-transporting ATPase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Carafoli, E.]]
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[[Category: Carafoli E]]
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[[Category: Diener, A.]]
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[[Category: Diener A]]
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[[Category: Elshorst, B.]]
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[[Category: Elshorst B]]
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[[Category: Foersterling, H.]]
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[[Category: Foersterling H]]
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[[Category: Griesinger, C.]]
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[[Category: Griesinger C]]
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[[Category: Hennig, M.]]
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[[Category: Hennig M]]
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[[Category: Krebs, J.]]
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[[Category: Krebs J]]
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[[Category: Maurer, M.]]
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[[Category: Maurer M]]
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[[Category: Schmid, H.]]
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[[Category: Schmid H]]
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[[Category: Schulte, P.]]
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[[Category: Schulte P]]
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[[Category: Schwalbe, H.]]
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[[Category: Schwalbe H]]
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[[Category: Vorherr, T.]]
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[[Category: Vorherr T]]
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[[Category: C20w]]
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[[Category: Calmodulin]]
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[[Category: Nmr]]
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[[Category: Plasma membrane calcium pump]]
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Current revision

NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP

PDB ID 1cff

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