Lysine-rich Cyclotides: A New Subclass of Circular Knotted Proteins from Violaceae
نویسندگان
چکیده
منابع مشابه
Distribution of circular proteins in plants: large-scale mapping of cyclotides in the Violaceae
During the last decade there has been increasing interest in small circular proteins found in plants of the violet family (Violaceae). These so-called cyclotides consist of a circular chain of approximately 30 amino acids, including six cysteines forming three disulfide bonds, arranged in a cyclic cystine knot (CCK) motif. In this study we map the occurrence and distribution of cyclotides throu...
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Several members of the Rubiaceae and Violaceae families produce a series of cyclotides or macrocyclic peptides of 29-31 amino acids with an embedded cystine knot. We aim to understand the mechanism of synthesis of cyclic peptides in plants and have isolated a cDNA clone that encodes the cyclotide kalata B1 as well as three other clones for related cyclotides from the African plant Oldenlandia a...
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Background Cyclotides are disulfide-rich miniproteins with the unique structural features of a circular backbone and knotted arrangement of three conserved disulfide bonds. These features make them exceptionally stable and they have applications as plant defense (insecticidal) agents and stable drug frameworks. So far they have been found mainly in two plant families, including in every species...
متن کاملEthnobotanical survey of Rinorea dentata (Violaceae) used in South-Western Nigerian ethnomedicine and detection of cyclotides
ETHNOPHARMACOLOGICAL RELEVANCE People living in the tropical rain forest of South-Western Nigeria use Rinorea dentata (P. Beauv.) Kuntze (Violaceae) in ethno-veterinary medicine to facilitate parturition. There are no evidence-based pharmacological investigations for the uterotonic activity of this plant. AIMS OF STUDY (i) Collection of data about the ethnopharmacological uses of R. dentata a...
متن کاملRefolding Process of Cysteine-Rich Proteins: Chitinase as a Model
Background: Recombinant proteins overexpressed in E. coli are usually deposited in inclusion bodies. Cysteines in the protein contribute to this process. Inter- and intra- molecular disulfide bonds in chitinase, a cysteine-rich protein, cause aggregation when the recombinant protein is overexpressed in E. coli. Hence, aggregated proteins should be solubilized and allowed to refold to obtain nat...
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ژورنال
عنوان ژورنال: ACS Chemical Biology
سال: 2015
ISSN: 1554-8929,1554-8937
DOI: 10.1021/acschembio.5b00454