1omg

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{{Seed}}
 
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[[Image:1omg.png|left|200px]]
 
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==NMR STUDY OF OMEGA-CONOTOXIN MVIIA==
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The line below this paragraph, containing "STRUCTURE_1omg", creates the "Structure Box" on the page.
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<StructureSection load='1omg' size='340' side='right'caption='[[1omg]]' 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'>[[1omg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_magus Conus magus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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, 13 models</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=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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{{STRUCTURE_1omg| PDB=1omg | 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=1omg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omg OCA], [https://pdbe.org/1omg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1omg RCSB], [https://www.ebi.ac.uk/pdbsum/1omg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1omg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O17A_CONMA O17A_CONMA] Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks Cav2.2/CACNA1B calcium channels (IC(50)=0.67-208 nM) (PubMed:26344359, PubMed:34589389, PubMed:7826361). It acts by neutralizing the outer electronegativity and sterically hindering the ion access path to the entrance of the channel selectivity filter (PubMed:34234349). It also shows antiproliferative effects on different glioma cell lines (M059J, U-138MG and U-251MG) (PubMed:28202361). In vivo, is lethal to fish (PubMed:26344359, PubMed:34589389). In vivo, injection into mammals induces adverse effects, such as tremor, diminution of spontaneous locomotor activity and bad coordinated locomotion (PubMed:26344359). In addition, it causes reduction of tumor area in the mouse glioma model, that is induced by the orthotopic injection of GL261 cells into the brain (PubMed:28202361).<ref>PMID:26344359</ref> <ref>PMID:34234349</ref> <ref>PMID:7826361</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The three-dimensional solution structure of omega-conotoxin MVIIA, a 25-mer peptide antagonist of N-type calcium channels, was determined by two-dimensional 1H NMR spectroscopy with simulated annealing calculations. A total of 13 converged structures of omega-conotoxin MVIIA were obtained on the basis of 273 experimental constraints, including 232 distance constraints obtained from nuclear Overhauser effect (NOE) connectivities, 22 torsion angle (phi, chi 1) constraints, and 19 constraints associated with hydrogen bonds and disulfide bonds. The atomic root mean square difference about the averaged coordinate positions is 0.47 +/- 0.08 A for the backbone atoms (N, C alpha, C) and 1.27 +/- 0.14 A for all heavy atoms of the entire peptide. The molecular structure of omega-conotoxin MVIIA is composed of a short triple-stranded antiparallel beta-sheet. The overall beta-sheet topology is +2x, -1, which is the same as that reported for omega-conotoxin GVIA, another N-type calcium channel blocker. The orientation of beta-stranded structure is similar to each other, suggesting that the conserved disulfide bond combination is essential for the molecular folding. We have recently determined by using alanine substitution analyses that Tyr 13 is essential for the activity of both toxins. On the basis of functional and structural analysis, it is shown that both omega-conotoxin MVIIA and GVIA retain a similar conformation to locate Tyr 13 in the appropriate position to allow binding to N-type calcium channels. These results provide a molecular basis for understanding the mechanism of calcium channel modulation through the toxin-channel interaction and insight into the discrimination of different subtypes of calcium channels.
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===NMR STUDY OF OMEGA-CONOTOXIN MVIIA===
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Three-dimensional structure in solution of the calcium channel blocker omega-conotoxin MVIIA.,Kohno T, Kim JI, Kobayashi K, Kodera Y, Maeda T, Sato K Biochemistry. 1995 Aug 15;34(32):10256-65. PMID:7640281<ref>PMID:7640281</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_7640281}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1omg" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 7640281 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_7640281}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1OMG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_magus Conus magus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMG OCA].
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==Reference==
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Three-dimensional structure in solution of the calcium channel blocker omega-conotoxin MVIIA., Kohno T, Kim JI, Kobayashi K, Kodera Y, Maeda T, Sato K, Biochemistry. 1995 Aug 15;34(32):10256-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7640281 7640281]
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[[Category: Conus magus]]
[[Category: Conus magus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kim, J I.]]
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[[Category: Kim J-I]]
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[[Category: Kobayashi, K.]]
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[[Category: Kobayashi K]]
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[[Category: Kodera, Y.]]
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[[Category: Kodera Y]]
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[[Category: Kohno, T.]]
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[[Category: Kohno T]]
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[[Category: Maeda, T.]]
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[[Category: Maeda T]]
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[[Category: Sato, K.]]
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[[Category: Sato K]]
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[[Category: Presynaptic neurotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:24:50 2008''
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Current revision

NMR STUDY OF OMEGA-CONOTOXIN MVIIA

PDB ID 1omg

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