3i5w

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

spinqualitylabelsall models 3i5w, resolution 1.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3i5w is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FLC Related: 1zmp, 3gny Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DEF5_HUMAN] Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing. Publication Abstract from PubMed 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. Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5.,de Leeuw E, Rajabi M, Zou G, Pazgier M, Lu W FEBS Lett. 2009 Aug 6;583(15):2507-12. Epub 2009 Jul 7. PMID:19589339 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Defensin 3D structures

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