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| | ==NMR STRUCTURE WITH TIGHTLY BOUND WATER MOLECULES OF CYTOTOXIN II (CARDIOTOXIN) FROM NAJA NAJA OXIANA IN AQUEOUS SOLUTION (MAJOR FORM).== | | ==NMR STRUCTURE WITH TIGHTLY BOUND WATER MOLECULES OF CYTOTOXIN II (CARDIOTOXIN) FROM NAJA NAJA OXIANA IN AQUEOUS SOLUTION (MAJOR FORM).== |
| - | <StructureSection load='1cb9' size='340' side='right'caption='[[1cb9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1cb9' size='340' side='right'caption='[[1cb9]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[1cb9]] 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=1CB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CB9 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1cb9]] 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=1CB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CB9 FirstGlance]. <br> |
| - | </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=1cb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cb9 OCA], [https://pdbe.org/1cb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cb9 RCSB], [https://www.ebi.ac.uk/pdbsum/1cb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cb9 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1cb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cb9 OCA], [https://pdbe.org/1cb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cb9 RCSB], [https://www.ebi.ac.uk/pdbsum/1cb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cb9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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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| | [[Category: Large Structures]] | | [[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: Bound water]]
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| - | [[Category: Cis/trans isomerization]]
| + | |
| - | [[Category: Membrane perturbation]]
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| - | [[Category: Toxin]]
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| 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
1H-NMR spectroscopy data, such as NOE intraprotein and (bound water)/protein contacts, 3J coupling constants and deuterium exchange rates were used to determine the in-solution spatial structure of cytotoxin II from Naja naja oxiana snake venom (CTII). Exploiting information from two 1H-NMR spectral components, shown to be due to cis/trans isomerization of the Val7-Pro8 peptide bond, spatial structures of CTII minor and major forms (1 : 6) were calculated using the torsion angle dynamics algorithm of the DYANA program and then energy refined using the FANTOM program. Each form, major and minor, is represented by 20 resulting conformers, demonstrating mean backbone rmsd values of 0.51 and 0.71 A, respectively. Two forms of CTII preserve the structural skeleton as three large loops, including two beta-sheets with bend regions, and demonstrate structural differences at loop I, where cis/trans isomerization occurs. The CTII side-chain distribution constitutes hydrophilic and hydrophobic belts around the protein, alternating in the trend of the three main loops. Because of the Omega-shaped backbone, formed in participation with two bound water molecules, the tip of loop II bridges the tips of loops I and III. This ensures the continuity of the largest hydrophobic belt, formed with the residues of these tips. Comparison revealed pronounced differences in the spatial organization of the tips of the three main loops between CTII and previous structures of homologous cytotoxins (cardiotoxins) in solution.
Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution: spatial structures with tightly bound water molecules.,Dementieva DV, Bocharov EV, Arseniev AS Eur J Biochem. 1999 Jul;263(1):152-62. PMID:10429199[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
- ↑ Dementieva DV, Bocharov EV, Arseniev AS. Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution: spatial structures with tightly bound water molecules. Eur J Biochem. 1999 Jul;263(1):152-62. PMID:10429199
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