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| | ==NMR STRUCTURE OF CARDIOTOXIN IN DPC-MICELLE== | | ==NMR STRUCTURE OF CARDIOTOXIN IN DPC-MICELLE== |
| - | <StructureSection load='1ffj' size='340' side='right' caption='[[1ffj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1ffj' size='340' side='right'caption='[[1ffj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ffj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Naja_oxiana Naja oxiana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FFJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ffj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_oxiana Naja oxiana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FFJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cb9|1cb9]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1ffj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffj OCA], [http://pdbe.org/1ffj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ffj RCSB], [http://www.ebi.ac.uk/pdbsum/1ffj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffj 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=1ffj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffj OCA], [https://pdbe.org/1ffj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ffj RCSB], [https://www.ebi.ac.uk/pdbsum/1ffj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CX2_NAJOX CX2_NAJOX]] This three-finger cytotoxin is a basic protein that interacts and penetrates into the cell membrane, with the tips of all the three loops. Cytotoxins which have a Pro-30 (P-type) interacts with membrane stronger that those which have a 'Ser-28' (S-type). CTII interacts with membrane stronger than CTI.<ref>PMID:11357394</ref> <ref>PMID:12709064</ref> <ref>PMID:15584897</ref> | + | [https://www.uniprot.org/uniprot/3SA2_NAJOX 3SA2_NAJOX] This three-finger cytotoxin is a basic protein that interacts and penetrates into the cell membrane, with the tips of all the three loops. Cytotoxins which have a Pro-30 (P-type) interacts with membrane stronger that those which have a 'Ser-28' (S-type). CTII interacts with membrane stronger than CTI.<ref>PMID:11357394</ref> <ref>PMID:12709064</ref> <ref>PMID:15584897</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/1ffj_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/1ffj_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1ffj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1ffj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cardiotoxin 3D structures|Cardiotoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Naja oxiana]] | | [[Category: Naja oxiana]] |
| - | [[Category: Arseniev, A S]] | + | [[Category: Arseniev AS]] |
| - | [[Category: Bocharov, E V]] | + | [[Category: Bocharov EV]] |
| - | [[Category: Dementieva, D V]] | + | [[Category: Dementieva DV]] |
| - | [[Category: Dubovskii, P V]] | + | [[Category: Dubovskii PV]] |
| - | [[Category: Utkin, Y N]] | + | [[Category: Utkin YN]] |
| - | [[Category: All-beta sheet protein]]
| + | |
| - | [[Category: Membrane perturbation]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
3SA2_NAJOX This three-finger cytotoxin is a basic protein that interacts and penetrates into the cell membrane, with the tips of all the three loops. Cytotoxins which have a Pro-30 (P-type) interacts with membrane stronger that those which have a 'Ser-28' (S-type). CTII interacts with membrane stronger than CTI.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Carditoxins (CTXs) from cobra snake venoms, the basic 60-62 residue all-beta sheet polypeptides, are known to bind to and impair the function of cell membranes. To assess the membrane induced conformation and orientation of CTXs, the interaction of the P-type cardiotoxin II from Naja oxiana snake venom (CTII) with perdeuterated dodecylphosphocholine (DPC) was studied using ( 1 )H-NMR spectroscopy and diffusion measurements. Under conditions where the toxin formed a well-defined complex with DPC, the spatial structure of CTII with respect to the presence of tightly bound water molecules in loop II, was calculated using the torsion angle dynamics program DYANA. The structure was found to be similar, except for subtle changes in the tips of all three loops, to the previously described "major" form of CTII in aqueous solution illustrated by the "trans" configuration of the Val7-Pro8 peptide bond. No "minor" form with the "cis" configuration of the above bond was found in the micelle-bound state. The broadening of the CTII backbone proton signals by 5, 16-doxylstearate relaxation probes, together with modeling based on the spatial structure of CTII, indicated a periphery mode of binding of the toxin molecule to the micelle and revealed its micelle interacting domain. The latter includes a hydrophobic region of CTII within the extremities of loops I and III (residues 5-11, 46-50), the basement of loop II (residues 24-29,31-37) and the belt of polar residues encircling these loops (lysines 4,5,12,23,50, serines 11,46, histidine 31, arginine 36). It is suggested that this structural motif and the mode of binding can be realized during interaction of CTXs with lipid and biological membranes.
Membrane binding motif of the P-type cardiotoxin.,Dubovskii PV, Dementieva DV, Bocharov EV, Utkin YN, Arseniev AS J Mol Biol. 2001 Jan 5;305(1):137-49. PMID:11114253[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dubinnyi MA, Dubovskii PV, Utkin IuN, Simonova TN, Barsukov LI, Arsen'ev AS. [ESR study of the interaction of cytotoxin II with model membranes]. Bioorg Khim. 2001 Mar-Apr;27(2):102-13. PMID:11357394
- ↑ Dubovskii PV, Lesovoy DM, Dubinnyi MA, Utkin YN, Arseniev AS. Interaction of the P-type cardiotoxin with phospholipid membranes. Eur J Biochem. 2003 May;270(9):2038-46. PMID:12709064
- ↑ Dubovskii PV, Lesovoy DM, Dubinnyi MA, Konshina AG, Utkin YN, Efremov RG, Arseniev AS. Interaction of three-finger toxins with phospholipid membranes: comparison of S- and P-type cytotoxins. Biochem J. 2005 May 1;387(Pt 3):807-15. PMID:15584897 doi:10.1042/BJ20041814
- ↑ Dubovskii PV, Dementieva DV, Bocharov EV, Utkin YN, Arseniev AS. Membrane binding motif of the P-type cardiotoxin. J Mol Biol. 2001 Jan 5;305(1):137-49. PMID:11114253 doi:10.1006/jmbi.2000.4283
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