1bf0
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf0 OCA], [http://www.ebi.ac.uk/pdbsum/1bf0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bf0 RCSB]</span> | ||
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[[Category: calcium channel blocker]] | [[Category: calcium channel blocker]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:59:35 2008'' |
Revision as of 15:59, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CALCICLUDINE (CAC) FROM GREEN MAMBA DENDROASPIS ANGUSTICEPS, NMR, 15 STRUCTURES
Overview
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.
About this Structure
1BF0 is a Single protein structure of sequence from Dendroaspis angusticeps. Full crystallographic information is available from OCA.
Reference
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
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