1kwi
Crystal Structure Analysis of the Cathelicidin Motif of ProtegrinsCrystal Structure Analysis of the Cathelicidin Motif of Protegrins
Structural highlights
FunctionPG3_PIG Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCathelicidins 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
|