1BAH
A TWO DISULFIDE DERIVATIVE OF CHARYBDOTOXIN WITH DISULFIDE 13-33 REPLACED BY TWO ALPHA-AMINOBUTYRIC ACIDS, NMR, 30 STRUCTURES
Summary for 1BAH
| Entry DOI | 10.2210/pdb1bah/pdb |
| Descriptor | CHARYBDOTOXIN (1 entity in total) |
| Functional Keywords | charybdotoxin, neurotoxin, potassium channel inhibitor, toxin |
| Biological source | Leiurus quinquestriatus (Egyptian scorpion) |
| Total number of polymer chains | 1 |
| Total formula weight | 4273.92 |
| Authors | Song, J.,Gilquin, B.,Jamin, N.,Guenneugues, M.,Dauplais, M.,Vita, C.,Menez, A. (deposition date: 1996-06-06, release date: 1997-01-11, Last modification date: 2020-01-15) |
| Primary citation | Song, J.,Gilquin, B.,Jamin, N.,Drakopoulou, E.,Guenneugues, M.,Dauplais, M.,Vita, C.,Menez, A. NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing. Biochemistry, 36:3760-3766, 1997 Cited by PubMed Abstract: The alpha/beta scorpion fold consisting of a short alpha-helix and beta-sheet is a structural motif common to scorpion toxins, insect defensins, and plant gamma-thionins that invariably contains three disulfides. CHABII is a two-disulfide derivative of the scorpion toxin charybdotoxin (ChTX), chemically synthesized by inserting two L-alpha-aminobutyric acids in place of the two half-cystine residues involved in the disulfide 13-33. This disulfide is one of the two disulfides which connect the alpha-helix to the beta-sheet. The solution structure of CHABII was determined at pH 6.3 and 5 degrees C using 2D NMR and simulated annealing from 513 distance and 46 dihedral angle constraints. The NMR structure of CHABII is well-defined as judged from the low value of the averaged backbone rms deviation between the 30 lowest energy structures and the energy-minimized mean structure ((rmsd) = 0.65 A for the entire sequence and 0.48 A for the segment 3-36). Analysis and comparison of the solution structures of CHABII and ChTX lead to the following conclusions: (i) the fold of CHABII is similar to that of ChTX as indicated by the low value of the averaged backbone atomic rms deviation between the 10 lowest energy solution structures of the two proteins (1.44 A); (ii) the packing of the hydrophobic core is well-preserved, underlying the critical structural role of the hydrophobic interactions even for such a small and cysteine-rich protein as ChTX. PubMed: 9092804DOI: 10.1021/bi962720h PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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