2MN3
Structure of Platypus 'Intermediate' Defensin-like Peptide (Int-DLP)
Summary for 2MN3
| Entry DOI | 10.2210/pdb2mn3/pdb |
| Related | 1b8w 1bnb 1zue |
| NMR Information | BMRB: 19878 |
| Descriptor | Defensin-BvL (1 entity in total) |
| Functional Keywords | defensin-like peptide, platypus defensin, beta-defensin, intermediate-dlp, antimicrobial protein |
| Biological source | Ornithorhynchus anatinus (duck-billed platypus,duckbill platypus) |
| Cellular location | Secreted (By similarity): P0C8B1 |
| Total number of polymer chains | 1 |
| Total formula weight | 5000.90 |
| Authors | Torres, A.M.,Bansal, P.S.,Koh, J.M.S.,Pages, G.,Wu, M.J.,Kuchel, P.W. (deposition date: 2014-03-27, release date: 2014-09-17, Last modification date: 2024-10-30) |
| Primary citation | Torres, A.M.,Bansal, P.,Koh, J.M.,Pages, G.,Wu, M.J.,Kuchel, P.W. Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide. Febs Lett., 588:1821-1826, 2014 Cited by PubMed Abstract: The three-dimensional structure of a chemically synthesized peptide that we have called 'intermediate' defensin-like peptide (Int-DLP), from the platypus genome, was determined by nuclear magnetic resonance (NMR) spectroscopy; and its antimicrobial activity was investigated. The overall structural fold of Int-DLP was similar to that of the DLPs and β-defensins, however the presence of a third antiparallel β-strand makes its structure more similar to the β-defensins than the DLPs. Int-DLP displayed potent antimicrobial activity against Staphylococcus aureus and Pseudomonas aeruginosa. The four arginine residues at the N-terminus of Int-DLP did not affect the overall fold, but were important for its antimicrobial potency. PubMed: 24694388DOI: 10.1016/j.febslet.2014.03.044 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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