Structure of the Cathelicidin Motif of Protegrin-3 Precursor: Structural Insights into the Activation Mechanism of an Antimicrobial Protein - Archive ouverte HAL Access content directly
Journal Articles Structure Year : 2002

Structure of the Cathelicidin Motif of Protegrin-3 Precursor: Structural Insights into the Activation Mechanism of an Antimicrobial Protein

Abstract

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.

Dates and versions

hal-02359517 , version 1 (12-11-2019)

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Jean-Frédéric Sanchez, François Hoh, Marie-Paule Strub, André Aumelas, Christian Dumas. Structure of the Cathelicidin Motif of Protegrin-3 Precursor: Structural Insights into the Activation Mechanism of an Antimicrobial Protein. Structure, 2002, 10, ⟨10.1016/S0969-2126(02)00859-6⟩. ⟨hal-02359517⟩
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