Oxidative folding of the cystine knot motif in cyclotide proteins

被引：21

作者：

Craik, DJ ^{[1
]}

Daly, NL ^{[1
]}

机构：

[1] Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia

来源：

PROTEIN AND PEPTIDE LETTERS | 2005年 / 12卷 / 02期

关键词：

circular proteins; cyclic peptides; kalata B1; NMR; conformational folding;

D O I：

10.2174/0929866053005863

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cyclotides are a large family of plant proteins that have a cyclic backbone and a knotted arrangement of three conserved disulfide bonds. Despite the apparent complexity of their cystine knot motif it is possible to efficiently fold these proteins, as exemplified by oxidative folding studies on the prototypic cyclotide, kalata B1. This mini-review reports on the current understanding of the folding process in cyclotides. The synthesis and folding of these molecules paves the way for their application as stable molecular templates.

引用

页码：147 / 152

页数：6

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