7npq

Crystal structure of the human LL37(17-29) I24C mutant antimicrobial peptide

spinqualitylabelsall models 7npq, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Human LL-3717-29 is an antimicrobial peptide forming thermostable supramolecular fibrils that surround bacterial cells. The crystal structure of LL-3717-29 bearing an I24C substitution of most buried position in the fibril revealed disulfide-bonded dimers that further assembled into a fibrillar structure of densely packed helices. We further demonstrated the position-dependent controllable antibacterial activity of LL-3717-29 I24C and other cysteine mutants, mediated by regulation of intermolecular disulfide bonds and their role in the formation of supramolecular structures. The morphology of the fibrils and their antibacterial mechanism of action might be dependent on their interactions with specific bacteria. The significant effect of disulfide bonds on the assembly into supramolecular structures and their sensitivity to reducing/oxidizing conditions may explain why short helical antimicrobial peptides with a single cysteine and an odd number of cysteines are selected against in nature. Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides.,Engelberg Y, Ragonis-Bachar P, Landau M Biomacromolecules. 2022 Jan 21. doi: 10.1021/acs.biomac.1c01353. PMID:35061360 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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