1bf0

<StructureSection load='1bf0' size='340' side='right'caption='[[1bf0]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>

</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=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>

[[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.

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== 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.

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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<div class="pdbe-citations 1bf0" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Desne, F]]

[[Category: Gilquin, B]]

[[Category: Guenneugues, M]]

[[Category: Lecoq, A]]

[[Category: Menez, A]]

[[Category: Zinn-Justin, S]]

[[Category: Calcium channel blocker]]