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'''Crystal Structure Analysis of the Cathelicidin Motif of Protegrins''' | '''Crystal Structure Analysis of the Cathelicidin Motif of Protegrins''' | ||
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[[Category: Sanchez, J F.]] | [[Category: Sanchez, J F.]] | ||
[[Category: Strub, M P.]] | [[Category: Strub, M P.]] | ||
[[Category: | [[Category: Cathelicidin motif]] | ||
[[Category: | [[Category: Disulfide]] | ||
[[Category: | [[Category: Mad]] | ||
[[Category: | [[Category: Protegrin]] | ||
[[Category: | [[Category: Selenocystine]] | ||
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Revision as of 20:15, 2 May 2008
Crystal Structure Analysis of the Cathelicidin Motif of Protegrins
Overview
Cathelicidins are a family of antimicrobial proteins isolated from leucocytes and epithelia cells that contribute to the innate host defense mechanisms in mammalians. Located in the C-terminal part of the holoprotein, the cathelicidin-derived antimicrobial peptide is liberated by a specific protease cleavage. Here, we report the X-ray structure of the cathelicidin motif of protegrin-3 solved by MAD phasing using the selenocysteine-labeled protein. Its overall structure represents a fold homologous to the cystatin family and adopts two native states, a monomer, and a domain-swapped dimer. This crystal structure is the first example of a structural characterization of the highly conserved cathelicidin motif and thus provides insights into the possible mechanism of activation of the antimicrobial protegrin peptide.
About this Structure
1KWI is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein., Sanchez JF, Hoh F, Strub MP, Aumelas A, Dumas C, Structure. 2002 Oct;10(10):1363-70. PMID:12377122 Page seeded by OCA on Fri May 2 23:15:27 2008
