5INZ
Racemic structure of baboon theta defensin-2
Summary for 5INZ
| Entry DOI | 10.2210/pdb5inz/pdb |
| Descriptor | Theta defensin-2, L-peptide, Theta defensin-2, D-peptide, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | cyclic peptide, mirror image beta sheet, antibiotic |
| Biological source | Papio anubis More |
| Total number of polymer chains | 4 |
| Total formula weight | 9373.50 |
| Authors | Wang, C.K.,King, G.J.,Conibear, A.C.,Ramos, M.C.,Craik, D.J. (deposition date: 2016-03-08, release date: 2016-04-27, Last modification date: 2024-10-16) |
| Primary citation | Wang, C.K.,King, G.J.,Conibear, A.C.,Ramos, M.C.,Chaousis, S.,Henriques, S.T.,Craik, D.J. Mirror Images of Antimicrobial Peptides Provide Reflections on Their Functions and Amyloidogenic Properties. J.Am.Chem.Soc., 138:5706-5713, 2016 Cited by PubMed Abstract: Enantiomeric forms of BTD-2, PG-1, and PM-1 were synthesized to delineate the structure and function of these β-sheet antimicrobial peptides. Activity and lipid-binding assays confirm that these peptides act via a receptor-independent mechanism involving membrane interaction. The racemic crystal structure of BTD-2 solved at 1.45 Å revealed a novel oligomeric form of β-sheet antimicrobial peptides within the unit cell: an antiparallel trimer, which we suggest might be related to its membrane-active form. The BTD-2 oligomer extends into a larger supramolecular state that spans the crystal lattice, featuring a steric-zipper motif that is common in structures of amyloid-forming peptides. The supramolecular structure of BTD-2 thus represents a new mode of fibril-like assembly not previously observed for antimicrobial peptides, providing structural evidence linking antimicrobial and amyloid peptides. PubMed: 27064294DOI: 10.1021/jacs.6b02575 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.447 Å) |
Structure validation
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