5MXL
Peptide-membrane interaction between targeting and lysis
Summary for 5MXL
| Entry DOI | 10.2210/pdb5mxl/pdb |
| NMR Information | BMRB: 34090 |
| Descriptor | GLY-LEU-PHE-ASP-ILE-VAL-LYS-LYS-VAL-VAL-GLY-ALA-LEU-GLY-NH2 (1 entity in total) |
| Functional Keywords | protein, cell cycle |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 1415.74 |
| Authors | Schneider, G.,Blatter, M. (deposition date: 2017-01-23, release date: 2017-02-22, Last modification date: 2024-10-09) |
| Primary citation | Stutz, K.,Muller, A.T.,Hiss, J.A.,Schneider, P.,Blatter, M.,Pfeiffer, B.,Posselt, G.,Kanfer, G.,Kornmann, B.,Wrede, P.,Altmann, K.H.,Wessler, S.,Schneider, G. Peptide-Membrane Interaction between Targeting and Lysis. ACS Chem. Biol., 12:2254-2259, 2017 Cited by PubMed Abstract: Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by "directed simulated evolution." The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides' membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide-membrane interaction. PubMed: 28763193DOI: 10.1021/acschembio.7b00504 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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