1bf0: Difference between revisions

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{{Seed}}
[[Image:1bf0.png|left|200px]]


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==CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15 STRUCTURES==
The line below this paragraph, containing "STRUCTURE_1bf0", creates the "Structure Box" on the page.
<StructureSection load='1bf0' size='340' side='right'caption='[[1bf0]]' 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'>[[1bf0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BF0 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, 15 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf0 OCA], [https://pdbe.org/1bf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bf0 RCSB], [https://www.ebi.ac.uk/pdbsum/1bf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bf0 ProSAT]</span></td></tr>
{{STRUCTURE_1bf0|  PDB=1bf0  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/VKTHC_DENAN VKTHC_DENAN] Potent blocker of high-voltage-activated calcium ion channels in the nanomolar range, particularly the L-type channels in cerebellar granule cells. The sensitivity of L-, N- and P-type channels to CAC is tissue and species-dependent. Blocks the L-type current of cardiac cells, depressing cardiac contractility.
== 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/bf/1bf0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1bf0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Calcicludine, a 60-amino acid protein isolated from the green mamba venom, has been recently identified as blocking a large set (i.e., L-, N- and P-type) of Ca2+ channels. The three-dimensional structure of calcicludine has been determined by NMR and molecular modeling using a data set of 723 unambiguous and 265 ambiguous distance restraints, as 33 phi and 13 chi1 dihedral angle restraints. Analysis of the 15 final structures (backbone root-mean-square deviation = 0.6 A) shows that calcicludine adopts the Kunitz-type protease inhibitor fold. Its three-dimensional structure is similar to that of snake K+ channel blockers dendrotoxins. Conformational differences with protease inhibitors and dendrotoxins are localized in the 3(10) helix and loop 1 (segments 1-7 and 10-19), the extremity of the beta-hairpin (segment 27-30), and loop 2 (segment 39-44). These regions correspond to the functional sites of bovine pancreatic trypsin inhibitor (BPTI) and dendrotoxins. The positioning of the N-terminal segment 1-7 relative to the rest of the protein is characteristic of calcicludine. The involvement of this segment and the positively charged K31 at the tip of the beta-hairpin in the biological activity of calcicludine is discussed.


===CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15 STRUCTURES===
Conformational and functional variability supported by the BPTI fold: solution structure of the Ca2+ channel blocker calcicludine.,Gilquin B, Lecoq A, Desne F, Guenneugues M, Zinn-Justin S, Menez A Proteins. 1999 Mar 1;34(4):520-32. PMID:10081964<ref>PMID:10081964</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_10081964}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1bf0" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 10081964 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_10081964}}
__TOC__
 
</StructureSection>
==About this Structure==
1BF0 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF0 OCA].
 
==Reference==
<ref group="xtra">PMID:10081964</ref><references group="xtra"/>
[[Category: Dendroaspis angusticeps]]
[[Category: Dendroaspis angusticeps]]
[[Category: Desne, F.]]
[[Category: Large Structures]]
[[Category: Gilquin, B.]]
[[Category: Desne F]]
[[Category: Guenneugues, M.]]
[[Category: Gilquin B]]
[[Category: Lecoq, A.]]
[[Category: Guenneugues M]]
[[Category: Menez, A.]]
[[Category: Lecoq A]]
[[Category: Zinn-Justin, S.]]
[[Category: Menez A]]
[[Category: Calcium channel blocker]]
[[Category: Zinn-Justin S]]
 
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