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==CARDIOTOXIN II FROM TAIWAN COBRA VENOM, NAJA NAJA ATRA: STRUCTURE IN SOLUTION AND COMPARISION AMONG HOMOLOGOUS CARDIOTOXINS==
==CARDIOTOXIN II FROM TAIWAN COBRA VENOM, NAJA NAJA ATRA: STRUCTURE IN SOLUTION AND COMPARISION AMONG HOMOLOGOUS CARDIOTOXINS==
<StructureSection load='1crf' size='340' side='right'caption='[[1crf]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''>
<StructureSection load='1crf' size='340' side='right'caption='[[1crf]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1crf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ansp_6988 Ansp 6988]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1crf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRF FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cre|1cre]]</div></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=1crf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1crf OCA], [https://pdbe.org/1crf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1crf RCSB], [https://www.ebi.ac.uk/pdbsum/1crf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1crf 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=1crf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1crf OCA], [https://pdbe.org/1crf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1crf RCSB], [https://www.ebi.ac.uk/pdbsum/1crf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1crf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/3SA2_NAJAT 3SA2_NAJAT]] Basic protein that binds to cell membrane and depolarizes cardiomyocytes. It also shows lytic activities, but 2-fold less important than that of CTX-A4. It binds to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity. It may interact with sulfatides in the cell membrane which induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It also may target the mitochondrial membrane and induce mitochondrial swelling and fragmentation.<ref>PMID:9398182</ref>
[https://www.uniprot.org/uniprot/3SA2_NAJAT 3SA2_NAJAT] Basic protein that binds to cell membrane and depolarizes cardiomyocytes. It also shows lytic activities, but 2-fold less important than that of CTX-A4. It binds to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity. It may interact with sulfatides in the cell membrane which induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It also may target the mitochondrial membrane and induce mitochondrial swelling and fragmentation.<ref>PMID:9398182</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1crf ConSurf].
</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=1crf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure in solution of cardiotoxin II, a membrane toxin from the venom of Taiwan cobra, Naja naja atra, was determined using 1H nuclear magnetic resonance spectroscopy and molecular modeling based on the hybrid distance geometry/dynamic simulated annealing technique. A complete sequence-specific proton assignment was obtained, and the secondary structures of the protein were determined from information on nuclear Overhauser effect connectivities, coupling constants, and hydrogen exchange were confirmed using the main-chain-directed strategy. Twelve simulated annealing structures found to be within a single family were selected based on the condition of distance constraint violation less than 0.02 nm and the dihedral angle violation less than 4 degrees. The average atomic root mean square deviation between the selected structures and their geometric average are 0.079 nm for the backbone atoms and 0.137 nm for all heavy atoms; they are 0.044 nm and 0.117 nm, respectively, when considering the secondary structural residues only. The molecule adopts a compact structure consisting of three major loops emerging from a globular head. These loops contain five strands to form double- and a triple-stranded antiparallel beta sheets. Comparisons are made between this structure and those of its homologous cardiotoxins in order to derive further information on their structural variations.
Cardiotoxin II from Taiwan cobra venom, Naja naja atra. Structure in solution and comparison among homologous cardiotoxins.,Bhaskaran R, Huang CC, Tsai YC, Jayaraman G, Chang DK, Yu C J Biol Chem. 1994 Sep 23;269(38):23500-8. PMID:8089116<ref>PMID:8089116</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1crf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ansp 6988]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bhaskaran, R]]
[[Category: Naja atra]]
[[Category: Chang, K D]]
[[Category: Bhaskaran R]]
[[Category: Huang, C C]]
[[Category: Chang KD]]
[[Category: Yu, C]]
[[Category: Huang CC]]
[[Category: Cardiotoxin]]
[[Category: Yu C]]

Revision as of 18:42, 13 March 2024

CARDIOTOXIN II FROM TAIWAN COBRA VENOM, NAJA NAJA ATRA: STRUCTURE IN SOLUTION AND COMPARISION AMONG HOMOLOGOUS CARDIOTOXINSCARDIOTOXIN II FROM TAIWAN COBRA VENOM, NAJA NAJA ATRA: STRUCTURE IN SOLUTION AND COMPARISION AMONG HOMOLOGOUS CARDIOTOXINS

Structural highlights

1crf is a 1 chain structure with sequence from Naja atra. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

3SA2_NAJAT Basic protein that binds to cell membrane and depolarizes cardiomyocytes. It also shows lytic activities, but 2-fold less important than that of CTX-A4. It binds to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity. It may interact with sulfatides in the cell membrane which induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It also may target the mitochondrial membrane and induce mitochondrial swelling and fragmentation.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Jang JY, Krishnaswamy T, Kumar S, Jayaraman G, Yang PW, Yu C. Comparison of the hemolytic activity and solution structures of two snake venom cardiotoxin analogues which only differ in their N-terminal amino acid. Biochemistry. 1997 Dec 2;36(48):14635-41. PMID:9398182 doi:10.1021/bi971107a
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