2N0V
Backbone 1H, Chemical Shift Assignments for Cn-APM1
Summary for 2N0V
| Entry DOI | 10.2210/pdb2n0v/pdb |
| NMR Information | BMRB: 25537 |
| Descriptor | Antimicrobial peptide 1 (1 entity in total) |
| Functional Keywords | antimicrobial protein |
| Biological source | Cocos nucifera (Coconut palm) |
| Cellular location | Secreted, extracellular space : P86705 |
| Total number of polymer chains | 1 |
| Total formula weight | 875.01 |
| Authors | Santana, M.J.,Oliveira, A.L.,Queiroz Jr., L.K.,Mandal, S.M.,Matos, C.O.,Dias, R.O.,Franco, O.L.,Liao, L.M. (deposition date: 2015-03-17, release date: 2015-12-23, Last modification date: 2024-11-20) |
| Primary citation | Santana, M.J.,de Oliveira, A.L.,Queiroz Junior, L.H.,Mandal, S.M.,Matos, C.O.,Dias, R.O.,Franco, O.L.,Liao, L.M. Structural insights into Cn-AMP1, a short disulfide-free multifunctional peptide from green coconut water. Febs Lett., 589:639-644, 2015 Cited by PubMed Abstract: Multifunctional and promiscuous antimicrobial peptides (AMPs) can be used as an efficient strategy to control pathogens. However, little is known about the structural properties of plant promiscuous AMPs without disulfide bonds. CD and NMR were used to elucidate the structure of the promiscuous peptide Cn-AMP1, a disulfide-free peptide isolated from green coconut water. Data here reported shows that peptide structure is transitory and could be different according to the micro-environment. In this regard, Cn-AMP1 showed a random coil in a water environment and an α-helical structure in the presence of SDS-d25 micelles. Moreover, deuterium exchange experiments showed that Gly4, Arg5 and Met9 residues are less accessible to solvent, suggesting that flexibility and cationic charges seem to be essential for Cn-AMP1 multiple activities. PubMed: 25639464DOI: 10.1016/j.febslet.2015.01.029 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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