1pg1

PROTEGRIN 1 (PG1) FROM PORCINE LEUKOCYTES, NMR, 20 STRUCTURES

spinqualitylabelsall models 1pg1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pg1 is a 1 chain structure with sequence from Sus scrofa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PG1_PIG Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro. Publication Abstract from PubMed BACKGROUND: The protegrins are a family of arginine- and cysteine-rich cationic peptides found in porcine leukocytes that exhibit a broad range of antimicrobial and antiviral activities. They are composed of 16-18 amino-acid residues including four cysteines, which form two disulfide linkages. To begin to understand the mechanism of action of these peptides, we set out to determine the structure of protegrin-1 (PG-1). RESULTS: We used two-dimensional homonuclear nuclear magnetic resonance spectroscopy to study the conformation of both natural and synthetic PG-1 under several conditions. A refined three-dimensional structure of synthetic PG-1 is presented. CONCLUSIONS: Both synthetic and natural protegrin-1 form a well-defined structure in solution composed primarily of a two-stranded antiparallel beta sheet, with strands connected by a beta turn. The structure of PG-1 suggests ways in which the peptide may interact with itself or other molecules to form the membrane pores and the large membrane-associated assemblages observed in protegrin-treated, gram-negative bacteria. Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes.,Fahrner RL, Dieckmann T, Harwig SS, Lehrer RI, Eisenberg D, Feigon J Chem Biol. 1996 Jul;3(7):543-50. PMID:8807886 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protegrin

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