FEBS Letters | |
Identification of an ion channel‐forming motif in the primary structure of tetanus and botulinum neurotoxins | |
Blewitt, Richard2  Montal, Mauricio2  Tomich, John M.1  Monta, Myrta S.2  | |
[1] Departments of Pediatrics and Biochemistry, University of Southern California Medical School and Children's Hospital, Los Angeles, CA 90054-0700, USA;Department of Biology, University of California San Diego, La Jolla, CA 92093-0319, USA | |
关键词: Tetanus toxin; Botulinum toxin; Ionic channel; Protein design; Lipid bilayer; Signal transduction; TeTx; tetanus toxin; BoTxA; botulinum neurotoxin serotype A; PC; 1; 2-diphytanoyl-sn-glycero-3-phosphocholine; τo; open times; τg; closed times; | |
DOI : 10.1016/0014-5793(92)81173-J | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Synthetic peptides with amino acid sequences corresponding to predicted transmembrane segments of tetanus toxin were used as probes to identify a channel-forming motif. A peptide denoted TeTx II, with sequence GVVLLLEYIPEITLPVIAALSIA, forms cation-selective channels when reconstituted in planar lipid bilayers. The single channel conductance in 0.5 M NaCl or KCl is 28 ± 3 and 24 ± 2 pS, respectively. In contrast, a peptide with sequence NFIGALETTGVVLLLEYIPEIT, denoted as TeTx I. or a peptide with the same amino acid composition as TeTx II but with a randomized sequence, do not form channels. Conformational energy calculations show that a bundle of four amphipathic α-helices is a plausible structural motif underlying observable pore properties. The identified functional module may account for the channel-forming activity of both tetanus toxin and the homologous botulinum toxin A.
【 授权许可】
Unknown
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