Circular proteins — no end in sight
| Autor: | Manuela Trabi, David J. Craik |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Protein Folding Sequence Homology Amino Acid Protein Conformation Molecular Sequence Data Cystine knot Cystine Knot Motifs Computational biology Biology Peptides Cyclic Biochemistry Cyclotide Protein structure Structural biology Cyclization Cyclotides Animals Humans Protein folding Amino Acid Sequence Structural motif Molecular Biology |
| Zdroj: | Trends in Biochemical Sciences. 27:132-138 |
| ISSN: | 0968-0004 |
| DOI: | 10.1016/s0968-0004(02)02057-1 |
| Popis: | Circular proteins are a recently discovered phenomenon. They presumably evolved to confer advantages over ancestral linear proteins while maintaining the intrinsic biological functions of those proteins. In general, these advantages include a reduced sensitivity to proteolytic cleavage and enhanced stability. In one remarkable family of circular proteins, the cyclotides, the cyclic backbone is additionally braced by a knotted arrangement of disulfide bonds that confers additional stability and topological complexity upon the family. This article describes the discovery, structure, function and biosynthesis of the currently known circular proteins. The discovery of naturally occurring circular proteins in the past few years has been complemented by new chemical and biochemical methods to make synthetic circular proteins; these are also briefly described. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect