2b5b
From Proteopedia
|
A reptilian defensin with anti-bacterial and anti-viral activity
Overview
Egg white of marine turtle Caretta caretta contains a small cationic, protein but lacks lysozyme. The protein was sequenced by a combination of, sequential Edman degradation, carboxypeptidase digestion, nuclear magnetic, resonance (NMR) and electrospray ionization tandem mass spectrometry. The, protein contains 36 amino acid residues of which six are half-cysteines., The three-dimensional structure of the protein was deduced from, two-dimensional NMR experiments and was observed to be similar to, vertebrate beta-defensins. However, disulfide connectivity is, C1-C6/C2-C5/C3-C4; different from that of the vertebrate beta-defensins., The protein showed strong antibacterial activity against Escherichia coli, and Salmonella typhimurium. The protein also showed significant antiviral, activity against an enveloped rhabdovirus, Chandipura virus, which is an, emerging human pathogen. This virus is also closely related to the, vesicular stomatitis virus, whose growth was also inhibited. This small, cationic protein is part of the innate immunity of this organism and, replaces lysozyme in the egg. It has the potential to be developed as an, antibacterial and antiviral agent.
About this Structure
2B5B is a Protein complex structure of sequences from Caretta caretta. Full crystallographic information is available from OCA.
Reference
Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity., Chattopadhyay S, Sinha NK, Banerjee S, Roy D, Chattopadhyay D, Roy S, Proteins. 2006 Aug 1;64(2):524-31. PMID:16700051
Page seeded by OCA on Tue Jan 29 18:17:11 2008
