Secreted Cysteine-Rich Repeat Proteins "SCREPs": A Novel Multi-Domain Architecture.

ABSTRACT: Peptide toxins isolated from animal venom secretions have proven to be useful pharmacological tools for probing the structure and function of a number of molecular receptors. Their molecular structures are stabilized by posttranslational formation of multiple disulfide bonds formed between sidechain thiols of cysteine residues, resulting in high thermal and chemical stability. Many of these peptides have been found to be potent modulators of ion channels, making them particularly influential in this field. Recently, several peptide toxins have been described that have an unusual tandem repeat organization, while also eliciting a unique pharmacological response toward ion channels. Most of these are two-domain peptide toxins from spider venoms, such as the double-knot toxin (DkTx), isolated

SUBMITTER: Maxwell M 

PROVIDER: S-EPMC6262176 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature