1KWI

Crystal Structure Analysis of the Cathelicidin Motif of Protegrins

1KWI の概要

• エントリーDOI: 10.2210/pdb1kwi/pdb
• 分子名称: Protegrin-3 Precursor (2 entities in total)
• 機能のキーワード: protegrin, cathelicidin motif, disulfide, mad, selenocystine, antimicrobial protein
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P32196
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11322.74

構造登録者

Sanchez, J.F.,Hoh, F.,Strub, M.P.,Aumelas, A.,Dumas, C. (登録日: 2002-01-29, 公開日: 2002-10-09, 最終更新日: 2024-11-20)

主引用文献

Sanchez, J.F.,Hoh, F.,Strub, M.P.,Aumelas, A.,Dumas, C.
Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein.
Structure, 10:1363-1370, 2002

PubMed 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.

PubMed: 12377122
DOI: 10.1016/S0969-2126(02)00859-6

実験手法

X-RAY DIFFRACTION (2.19 Å)