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{{STRUCTURE_1kwi|  PDB=1kwi  |  SCENE=  }}  
{{STRUCTURE_1kwi|  PDB=1kwi  |  SCENE=  }}  


'''Crystal Structure Analysis of the Cathelicidin Motif of Protegrins'''
===Crystal Structure Analysis of the Cathelicidin Motif of Protegrins===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Protegrin]]
[[Category: Protegrin]]
[[Category: Selenocystine]]
[[Category: Selenocystine]]
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Revision as of 08:09, 2 July 2008

File:1kwi.png

Template:STRUCTURE 1kwi

Crystal Structure Analysis of the Cathelicidin Motif of Protegrins

Template:ABSTRACT PUBMED 12377122

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

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