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2MN3

Structure of Platypus 'Intermediate' Defensin-like Peptide (Int-DLP)

Summary for 2MN3
Entry DOI10.2210/pdb2mn3/pdb
Related1b8w 1bnb 1zue
NMR InformationBMRB: 19878
DescriptorDefensin-BvL (1 entity in total)
Functional Keywordsdefensin-like peptide, platypus defensin, beta-defensin, intermediate-dlp, antimicrobial protein
Biological sourceOrnithorhynchus anatinus (duck-billed platypus,duckbill platypus)
Cellular locationSecreted (By similarity): P0C8B1
Total number of polymer chains1
Total formula weight5000.90
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 citationTorres, 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: 24694388
DOI: 10.1016/j.febslet.2014.03.044
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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