Post-translationally modified neuropeptides from Conus venoms.
Predatory cone snails (genus Conus) comprise what is arguably the largest living genus of marine animals (500 species). All Conus use complex venoms to capture prey and for other biological purposes. Most biologically active components of these venoms are small disulfide-rich peptides, generally 7-35 amino acids in length. There are probably of the order of 100 different peptides expressed in the venom of each of the 500 Conus species [1,2]. Peptide sequences diverge rapidly between Conus species, resulting in a distinct peptide complement for each species. Thus, the genus as a whole has probably generated approximately 50 000 different peptides, which can be organized into families and superfamilies with shared sequence elements [3]. In this minireview, we provide a brief overview of the neuropharmacological, molecular and cell-biological aspects of the Conus peptides. However, the major focus of the review will be the remarkable array of post-translational modifications found in these peptides.
Craig
A G
AG
The Clayton Foundation Laboratory for Peptide Biology, The Salk Institute, La Jolla, CA, USA.
Bandyopadhyay
P
P
Olivera
B M
BM
D000595:Amino Acid Sequence; D000818:Animals; D018698:Glutamic Acid / Q000378:metabolism; D007473:Ion Channels / Q000378:metabolism; D007536:Isomerism; D008969:Molecular Sequence Data; D008978:Mollusk Venoms / Q000737:chemistry*; D009479:Neuropeptides / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D012908:Snails; D014443:Tyrosine / Q000737:chemistry
D007473:Ion Channels; D008978:Mollusk Venoms; D009479:Neuropeptides; D018698:Glutamic Acid; D014443:Tyrosine