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[[Image:1cvo.jpg|left|200px]]


{{Structure
==THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA==
|PDB= 1cvo |SIZE=350|CAPTION= <scene name='initialview01'>1cvo</scene>
<StructureSection load='1cvo' size='340' side='right'caption='[[1cvo]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1cvo]] 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=1CVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CVO FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvo OCA], [https://pdbe.org/1cvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cvo RCSB], [https://www.ebi.ac.uk/pdbsum/1cvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cvo ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/3SOF5_NAJAT 3SOF5_NAJAT] Non-cytotoxic protein that does not show lytic and hemolytic activities, but can induce aggregation and fusion of sphingomyelin vesicles (PubMed:8182052). It binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with high affinity, and it inhibits osteoclast differentiation and bone resorption in mice, probably due to binding to integrin alpha-V/beta-3 (PubMed:16407244).<ref>PMID:14743531</ref> <ref>PMID:16407244</ref> <ref>PMID:8182052</ref> <ref>PMID:8703922</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cvo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1cvo ConSurf].
<div style="clear:both"></div>


'''THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA'''
==See Also==
 
*[[Cardiotoxin 3D structures|Cardiotoxin 3D structures]]
 
== References ==
==Overview==
<references/>
Cardiotoxins are small proteins that are found in the venoms of snakes from the Elapidae family. These toxins are known to bind to and disrupt the organization, integrity, and function of the cell membrane. Most of the well-studied cardiotoxins cause depolarization of membrane potentials and/or lysis of red cells. In contrast, CTX V from Naja naja atra displays poor hemolytic activity but is proficient at inducing aggregation and fusion of sphingomyelin vesicles [Chien et al. (1991) J. Biol. Chem. 266, 3252-3259]. To determine whether the unique activity of this CTX is attributable to its tertiary structure, the solution structure of CTX V was determined by NMR methods. On the basis of these studies, this cardiotoxin has the same general topology as other members of the family, and thus its unusual properties do not arise from any gross structural differences that are detectable by solution NMR methods. Molecular dynamics calculations indicate that residues 36-50 show concerted fluctuations. On the basis of sequence similarity, we postulate that residues 30-34 are important in determining the specificity of cardiotoxins for fusion versus lysis of vesicles.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1CVO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVO OCA].
 
==Reference==
Solution structure of cardiotoxin V from Naja naja atra., Singhal AK, Chien KY, Wu WG, Rule GS, Biochemistry. 1993 Aug 10;32(31):8036-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8347605 8347605]
[[Category: Naja atra]]
[[Category: Naja atra]]
[[Category: Single protein]]
[[Category: Chien K-Y]]
[[Category: Chien, K Y.]]
[[Category: Rule GS]]
[[Category: Rule, G S.]]
[[Category: Singhal AK]]
[[Category: Singhal, A K.]]
[[Category: Wu W-G]]
[[Category: Wu, W G.]]
[[Category: cytotoxin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:29 2008''

Latest revision as of 18:43, 13 March 2024

THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRATHE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA

Structural highlights

1cvo 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

3SOF5_NAJAT Non-cytotoxic protein that does not show lytic and hemolytic activities, but can induce aggregation and fusion of sphingomyelin vesicles (PubMed:8182052). It binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with high affinity, and it inhibits osteoclast differentiation and bone resorption in mice, probably due to binding to integrin alpha-V/beta-3 (PubMed:16407244).[1] [2] [3] [4]

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. ↑ Konshina AG, Volynskii PE, Arsen'ev AS, Efremov RG. [Interaction of cardiotoxin A5 with a membrane: role of conformational heterogeneity and hydrophilic properties] Bioorg Khim. 2003 Nov-Dec;29(6):577-88. PMID:14743531
  2. ↑ Wu PL, Lee SC, Chuang CC, Mori S, Akakura N, Wu WG, Takada Y. Non-cytotoxic cobra cardiotoxin A5 binds to alpha(v)beta3 integrin and inhibits bone resorption. Identification of cardiotoxins as non-RGD integrin-binding proteins of the Ly-6 family. J Biol Chem. 2006 Mar 24;281(12):7937-45. Epub 2006 Jan 10. PMID:16407244 doi:http://dx.doi.org/M513035200
  3. ↑ Chien KY, Chiang CM, Hseu YC, Vyas AA, Rule GS, Wu W. Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions. J Biol Chem. 1994 May 20;269(20):14473-83. PMID:8182052
  4. ↑ Chiang CM, Chien KY, Lin HJ, Lin JF, Yeh HC, Ho PL, Wu WG. Conformational change and inactivation of membrane phospholipid-related activity of cardiotoxin V from Taiwan cobra venom at acidic pH. Biochemistry. 1996 Jul 16;35(28):9167-76. PMID:8703922 doi:http://dx.doi.org/10.1021/bi952823k
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