1LXE

CRYSTAL STRUCTURE OF THE CATHELICIDIN MOTIF OF PROTEGRINS

Summary for 1LXE

• Entry DOI: 10.2210/pdb1lxe/pdb
• Related: 1kwi
• Descriptor: protegrin-3 precursor (2 entities in total)
• Functional Keywords: protegrin, cathelicidin motif, disulfide, domain swapping, antimicrobial protein
• Biological source: Sus scrofa (pig)
• Cellular location: Secreted: P32196
• Total number of polymer chains: 1
• Total formula weight: 11322.74

Authors

Sanchez, J.F.,Hoh, F.,Strub, M.P.,Aumelas, A.,Dumas, C. (deposition date: 2002-06-05, release date: 2002-10-09, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)