7NPQ
Crystal structure of the human LL37(17-29) I24C mutant antimicrobial peptide
Summary for 7NPQ
| Entry DOI | 10.2210/pdb7npq/pdb |
| Descriptor | Cathelicidin antimicrobial peptide (2 entities in total) |
| Functional Keywords | ll-37, functional fibril, helical fibril, amps, cys mutant, design, antimicrobial peptide, antimicrobial protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 3428.22 |
| Authors | Landau, M.,Engelberg, Y. (deposition date: 2021-02-28, release date: 2022-02-16, Last modification date: 2024-11-06) |
| Primary citation | Engelberg, Y.,Ragonis-Bachar, P.,Landau, M. Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides. Biomacromolecules, 23:926-936, 2022 Cited by PubMed Abstract: Human LL-37 is an antimicrobial peptide forming thermostable supramolecular fibrils that surround bacterial cells. The crystal structure of LL-37 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-37 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. PubMed: 35061360DOI: 10.1021/acs.biomac.1c01353 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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