3I5W

Crystal structure of human alpha-defensin 5 (mutant R13H)

Summary for 3I5W

• Entry DOI: 10.2210/pdb3i5w/pdb
• Related: 1ZMP 3GNY
• Descriptor: Defensin-5, CITRATE ANION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: human alpha-defensin 5, hd5, antimicrobial peptide, antibiotic, antimicrobial, defensin, disulfide bond, fungicide, secreted, antimicrobial protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: Q01523
• Total number of polymer chains: 2
• Total formula weight: 7374.92

Authors

Pazgier, M.,Lu, W. (deposition date: 2009-07-06, release date: 2009-07-28, Last modification date: 2024-11-06)

Primary citation

de Leeuw, E.,Rajabi, M.,Zou, G.,Pazgier, M.,Lu, W.
Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5
Febs Lett., 583:2507-2512, 2009

PubMed Abstract: Defensins constitute a major family of natural antimicrobial peptides that protect the host against microbial invasion. Here, we report on the antibacterial properties and cellular interaction of Human Defensin 5 as a function of its positive charge and hydrophobicity. We find that selective replacement of arginine residues in HD-5 by alanine or charge-neutral lysine residues reduces antibacterial killing as well as host cell interaction. We identify arginines at positions 9 and 28 in the HD-5 sequence as particularly important for its function. Replacement of arginine at position 13 to Histidine, as observed in a Crohn's disease patient, reduced bacterial killing strain-selectively. Finally, we find that HD-5 interacts with host cells via receptor-mediated mechanisms.

PubMed: 19589339
DOI: 10.1016/j.febslet.2009.06.051

Experimental method

X-RAY DIFFRACTION (1.63 Å)