1omg

From Proteopedia

(Difference between revisions)

Revision as of 09:58, 12 May 2021

NMR STUDY OF OMEGA-CONOTOXIN MVIIA

Structural highlights

1omg is a 1 chain structure with sequence from Conus magus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CO17A_CONMA] Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks N-type calcium channels (Cav2.2/CACNA1B).

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kohno T, Kim JI, Kobayashi K, Kodera Y, Maeda T, Sato K. Three-dimensional structure in solution of the calcium channel blocker omega-conotoxin MVIIA. Biochemistry. 1995 Aug 15;34(32):10256-65. PMID:7640281

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1omg"

@@ Line 3: / Line 3: @@
 <StructureSection load='1omg' size='340' side='right'caption='[[1omg]], [[NMR_Ensembles_of_Models | 13 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1omg]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OMG FirstGlance]. <br>
+<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>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1omg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omg OCA], [http://pdbe.org/1omg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1omg RCSB], [http://www.ebi.ac.uk/pdbsum/1omg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1omg ProSAT]</span></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=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>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CO17A_CONMA CO17A_CONMA]] Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks N-type calcium channels (Cav2.2/CACNA1B).
+[[https://www.uniprot.org/uniprot/CO17A_CONMA CO17A_CONMA]] Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks N-type calcium channels (Cav2.2/CACNA1B).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1omg

From Proteopedia

Revision as of 09:58, 12 May 2021

NMR STUDY OF OMEGA-CONOTOXIN MVIIA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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