1lxe
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(New page: 200px<br /><applet load="1lxe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxe, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 18:50, 20 November 2007
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CRYSTAL STRUCTURE 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
1LXE 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
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