2N65
Disulphide linked homodimer of designed antimicrobial peptide VG16KRKP
Summary for 2N65
| Entry DOI | 10.2210/pdb2n65/pdb |
| Related | 2N63 |
| NMR Information | BMRB: 25751 |
| Descriptor | antimicrobial peptide VG16KRKP (1 entity in total) |
| Functional Keywords | disulphide linked vg16krkp homodimer, designed antimicrobial peptide, de novo protein, antimicrobial protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 2 |
| Total formula weight | 3530.31 |
| Authors | Datta, A.,Bhunia, A. (deposition date: 2015-08-12, release date: 2016-03-23, Last modification date: 2024-10-30) |
| Primary citation | Datta, A.,Kundu, P.,Bhunia, A. Designing potent antimicrobial peptides by disulphide linked dimerization and N-terminal lipidation to increase antimicrobial activity and membrane perturbation: Structural insights into lipopolysaccharide binding. J Colloid Interface Sci, 461:335-345, 2016 Cited by PubMed Abstract: The remarkable rise in multi-drug resistant Gram-negative bacterial pathogens is a major concern to the well being of humans as well as susceptible plants. In recent years, diseases associated with inflammation and septicemia have already become a global health issue. Therefore, there is a rising demand for the development of novel "super" antibiotics. In this context, antimicrobial peptides offer an attractive, alternate therapeutic solution to conventional antibiotics. PubMed: 26407061DOI: 10.1016/j.jcis.2015.09.036 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
