1mtx
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DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF MARGATOXIN BY 1H, 13C, 15N TRIPLE-RESONANCE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
OverviewOverview
The solution structure of the 39-residue peptide margatoxin, a scorpion, toxin that selectively blocks the voltage-gated potassium-channel Kv1.3, has been determined by NMR spectroscopy. The toxin was isotopically, labeled with 13C and 15N and studied using two-dimensional homonuclear and, three- and four-dimensional heteronuclear NMR spectroscopy. The final, structure was determined using 501 constraints, comprising 422 NOE, constraints, 60 dihedral angle constraints, 9 disulfide constraints, and, 10 hydrogen bond constraints. Structures were initially determined with, the program PEGASUS and subsequently refined with X-PLOR. The average rms, deviation from a calculated average structure for the backbone atoms of, residues 3-38 is 0.40 A. A helix is present from residues 11 to 20 and, includes two proline residues at positions 15 and 16. A loop at residues, 21-24 leads into a two-strand antiparallel sheet from residues 25 to 38, with a turn at residues 30-33. Residues 3-6 run adjacent to the 33-38, strand but do not form a canonical beta-strand. The two additional, residues of margatoxin, relative to the related toxins charybdotoxin and, iberiotoxin, insert in a manner that extends the beta-sheet by one, residue. Otherwise, the global structure is very similar to that of these, two other toxins. The longer sheet may have implications for channel, selectivity.
About this StructureAbout this Structure
1MTX is a Single protein structure of sequence from Centruroides margaritatus. Full crystallographic information is available from OCA.
ReferenceReference
Determination of the three-dimensional structure of margatoxin by 1H, 13C, 15N triple-resonance nuclear magnetic resonance spectroscopy., Johnson BA, Stevens SP, Williamson JM, Biochemistry. 1994 Dec 20;33(50):15061-70. PMID:7999764
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