1cvo
From Proteopedia
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==THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA== | ==THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA== | ||
| - | <StructureSection load='1cvo' size='340' side='right' caption='[[1cvo | + | <StructureSection load='1cvo' size='340' side='right'caption='[[1cvo]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1cvo]] is a 1 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cvo_consurf.spt"</scriptWhenChecked> | + | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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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=1cvo 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=1cvo ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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:8347605<ref>PMID:8347605</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1cvo" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Cardiotoxin 3D structures|Cardiotoxin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Chien | + | [[Category: Naja atra]] |
| - | [[Category: Rule | + | [[Category: Chien K-Y]] |
| - | [[Category: Singhal | + | [[Category: Rule GS]] |
| - | [[Category: Wu | + | [[Category: Singhal AK]] |
| - | + | [[Category: Wu W-G]] | |
Current revision
THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA
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Categories: Large Structures | Naja atra | Chien K-Y | Rule GS | Singhal AK | Wu W-G
