Ontology highlight
ABSTRACT:
SUBMITTER: Berkut AA
PROVIDER: S-EPMC4281751 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Berkut Antonina A AA Peigneur Steve S Myshkin Mikhail Yu MY Paramonov Alexander S AS Lyukmanova Ekaterina N EN Arseniev Alexander S AS Grishin Eugene V EV Tytgat Jan J Shenkarev Zakhar O ZO Vassilevski Alexander A AA
The Journal of biological chemistry 20141028 1
We present a structural and functional study of a sodium channel activation inhibitor from crab spider venom. Hm-3 is an insecticidal peptide toxin consisting of 35 amino acid residues from the spider Heriaeus melloteei (Thomisidae). We produced Hm-3 recombinantly in Escherichia coli and determined its structure by NMR spectroscopy. Typical for spider toxins, Hm-3 was found to adopt the so-called "inhibitor cystine knot" or "knottin" fold stabilized by three disulfide bonds. Its molecule is amph ...[more]