1bf0

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

1bf0 is a 1 chain structure with sequence from Dendroaspis angusticeps. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 15 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gilquin B, Lecoq A, Desne F, Guenneugues M, Zinn-Justin S, Menez A. Conformational and functional variability supported by the BPTI fold: solution structure of the Ca2+ channel blocker calcicludine. Proteins. 1999 Mar 1;34(4):520-32. PMID:10081964

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bf0"

@@ Line 1: / Line 1: @@
 ==CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15 STRUCTURES==
-<StructureSection load='1bf0' size='340' side='right'caption='[[1bf0]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+<StructureSection load='1bf0' size='340' side='right'caption='[[1bf0]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bf0]] is a 1 chain structure. 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>
+<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>
-</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>
+</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>
+<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>
 </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.
+[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]]
@@ Line 13: / Line 14: @@
   <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/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Dendroaspis angusticeps]]
 [[Category: Large Structures]]
-[[Category: Desne, F]]
+[[Category: Desne F]]
-[[Category: Gilquin, B]]
+[[Category: Gilquin B]]
-[[Category: Guenneugues, M]]
+[[Category: Guenneugues M]]
-[[Category: Lecoq, A]]
+[[Category: Lecoq A]]
-[[Category: Menez, A]]
+[[Category: Menez A]]
-[[Category: Zinn-Justin, S]]
+[[Category: Zinn-Justin S]]
-[[Category: Calcium channel blocker]]

1bf0

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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