1cvo: Difference between revisions

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-[[Image:1cvo.jpg|left|200px]]
-<!--
+==THE SOLUTION STRUCTURE OF CARDIOTOXIN V FROM NAJA NAJA ATRA==
-The line below this paragraph, containing "STRUCTURE_1cvo", creates the "Structure Box" on the page.
+<StructureSection load='1cvo' size='340' side='right'caption='[[1cvo]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1cvo|  PDB=1cvo  |  SCENE=  }}
+</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]]
-CVO 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: 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 Fri May  2 13:09:40 2008''