2mfs | pdb_00002mfs

Solution NMR structure of the cactus-derived antimicrobial peptide Ep-AMP1

spinqualitylabelsall models 2mfs, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mfs is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Naturally occurring cystine knot peptides show a wide range of biological activity, and as they have inherent stability they represent potential scaffolds for peptide-based drug design and biomolecular engineering. Here we report the discovery, sequencing, chemical synthesis, three-dimensional solution structure determination and bioactivity of the first cystine knot peptide from Cactaceae (cactus) family: Ep-AMP1 from Echinopsis pachanoi. The structure of Ep-AMP1 (35 amino acids) conforms to that of the inhibitor cystine knot (or knottin) family but represents a novel diverse sequence; its activity was more than 500 times higher against bacterial than against eukaryotic cells. Rapid bactericidal action and liposome leakage implicate membrane permeabilisation as the mechanism of action. Sequence homology places Ec-AMP1 in the plant C6-type of antimicrobial peptides, but the three dimensional structure is highly similar to that of a spider neurotoxin. A Cactus-Derived Toxin-Like Cystine Knot Peptide with Selective Antimicrobial Activity.,Aboye TL, Stromstedt AA, Gunasekera S, Bruhn JG, El-Seedi H, Rosengren KJ, Goransson U Chembiochem. 2015 Mar 27. doi: 10.1002/cbic.201402704. PMID:25821084 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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