Abstract:
:Maurotoxin (MTX) is a 34-residue toxin that has been isolated from the venom of the chactidae scorpion Scorpio maurus palmatus, and characterized. Together with Pi1 and HsTx1, MTX belongs to a family of short-chain four-disulfide-bridged scorpion toxins acting on potassium channels. However, contrary to other members of this family, MTX exhibits an uncommon disulfide bridge organization of the type C1-C5, C2-C6, C3-C4 and C7-C8, versus C1-C5, C2-C6, C3-C7 and C4-C8 for both Pi1 and HsTx1. Here, we report that the substitution of MTX proline residues located at positions 12 and/or 20, adjacent to C3 (Cys(13)) and C4 (Cys(19)), results in conventional Pi1- and HsTx1-like arrangement of the half-cystine pairings. In this case, this novel disulfide bridge arrangement is without obvious incidence on the overall three-dimensional structure of the toxin. Pharmacological assays of this structural analog, [A(12),A(20)]MTX, reveal that the blocking activities on Shaker B and rat Kv1.2 channels remain potent whereas the peptide becomes inactive on rat Kv1.3. These data indicate, for the first time, that discrete point mutations in MTX can result in a marked reorganization of the half-cystine pairings, accompanied with a novel pharmacological profile for the analog.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Carlier E,Fajloun Z,Mansuelle P,Fathallah M,Mosbah A,Oughideni R,Sandoz G,Di Luccio E,Geib S,Regaya I,Brocard J,Rochat H,Darbon H,Devaux C,Sabatier JM,de Waard Mdoi
10.1016/s0014-5793(00)02433-9keywords:
subject
Has Abstractpub_date
2001-02-02 00:00:00pages
202-7issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02433-9journal_volume
489pub_type
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