1bf0

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[[Image:1bf0.gif|left|200px]]
 
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{{Structure
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==CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15 STRUCTURES==
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|PDB= 1bf0 |SIZE=350|CAPTION= <scene name='initialview01'>1bf0</scene>
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<StructureSection load='1bf0' size='340' side='right'caption='[[1bf0]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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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|GENE=
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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>
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}}
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</table>
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== Function ==
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'''CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15 STRUCTURES'''
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bf0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1bf0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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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.
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.
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==About this Structure==
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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>
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1BF0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF0 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10081964 10081964]
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</div>
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<div class="pdbe-citations 1bf0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Dendroaspis angusticeps]]
[[Category: Dendroaspis angusticeps]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Desne, F.]]
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[[Category: Desne F]]
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[[Category: Gilquin, B.]]
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[[Category: Gilquin B]]
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[[Category: Guenneugues, M.]]
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[[Category: Guenneugues M]]
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[[Category: Lecoq, A.]]
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[[Category: Lecoq A]]
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[[Category: Menez, A.]]
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[[Category: Menez A]]
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[[Category: Zinn-Justin, S.]]
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[[Category: Zinn-Justin S]]
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[[Category: calcium channel blocker]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:07 2008''
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Current revision

CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15 STRUCTURES

PDB ID 1bf0

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