Circular proteins and mechanisms of cyclization

Conlan, Brendon F., Gillon, Amanda D., Craik, David J. and Anderson, Marilyn A. (2010). Circular proteins and mechanisms of cyclization. In: Proceedings of the 1st International Conference on Circular Proteins. 1st International Conference on Circular Proteins, Heron Island, Qld, Australia, (573-583). 18-21 October, 2009. doi:10.1002/bip.21422


Author Conlan, Brendon F.
Gillon, Amanda D.
Craik, David J.
Anderson, Marilyn A.
Title of paper Circular proteins and mechanisms of cyclization
Conference name 1st International Conference on Circular Proteins
Conference location Heron Island, Qld, Australia
Conference dates 18-21 October, 2009
Proceedings title Proceedings of the 1st International Conference on Circular Proteins   Check publisher's open access policy
Journal name Peptide Science   Check publisher's open access policy
Place of Publication Hoboken, NJ, U.S.A
Publisher Wiley Interscience
Publication Year 2010
Year available 2010
Sub-type Fully published paper
DOI 10.1002/bip.21422
ISSN 0006-3525
1069-2630
1097-0282
Volume 94
Issue 5
Start page 573
End page 583
Total pages 11
Collection year 2011
Language eng
Abstract/Summary Cyclization via head-to-tail linkage of the termini of a peptide chain occurs in only a small percentage of proteins, but engenders the resultant cyclic proteins with exceptional stability. The mechanisms involved are poorly understood and this review attempts to summarize what is known of the events that lead to cyclization. Cyclic proteins are found in both prokaryotic and eukaryotic species. The prokaryotic circular proteins include the bacteriocins and pilins. The eukaryotic circular proteins in mammals include the theta defensins, found in rhesus macaques, and the retrocyclins. Two types of cyclic proteins have been found in plants, the sunflower trypsin inhibitor and the larger, more prolific, group known as cyclotides. The cyclotides from Oldenlandia affinis, the plant in which these cyclotides were first discovered, are processed by an asparaginyl endopeptidase which is a cysteine protease. Cysteine proteases are commonly associated with transpeptidation reactions, which, for suitable substrates can lead to cyclization events. These proteases cleave an amide bond and form an acyl enzyme intermediate before nucleophilic attack by the amine group of the N-terminal residue to form a peptide bond, resulting in a cyclic peptide. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 573–583, 2010.
Keyword Circular protein
Cyclotide
Peptide
Protein cyclization
Post-translational modification
Transpeptidation
Cysteine protease
Asparaginyl endopeptidase
AEP
VPE
Kalata
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Peptide Science, Special Issue: Special Issue on International Conference on Circular Proteins, Article first published online: 4 August, 2010.

 
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Created: Tue, 01 Feb 2011, 11:59:15 EST by Susan Allen on behalf of Institute for Molecular Bioscience