2mz6

NMR structure of Protegrin-3 (PG3) in the presence of DPC micelles

spinqualitylabelsall models 2mz6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mz6 is a 2 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, 1 model Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PG3_PIG Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro. Publication Abstract from PubMed A tendency to dimerize in the presence of lipids was found for the protegrin. The dimer formation by the protegrin-1 (PG-1) is the first step for further oligomeric membrane pore formation. Generally there are two distinct model of PG-1 dimerization in either a parallel or antiparallel beta-sheet. But despite the wealth of data available today, protegrin dimer structure and pore formation is still not completely understood. In order to investigate a more detailed dimerization process of PG-1 and if it will be the same for another type of protegrins, in this work we used a high-resolution NMR spectroscopy for structure determination of protegrin-3 (RGGGL-CYCRR-RFCVC-VGR) in the presence of perdeuterated DPC micelles and demonstrate that PG-3 forms an antiparallel NCCN dimer with a possible association of these dimers. This structural study complements previously published solution, solid state and computational studies of PG-1 in various environments and validate the potential of mean force simulations of PG-1 dimers and association of dimers to form octameric or decameric beta-barrels. Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.,Usachev KS, Efimov SV, Kolosova OA, Klochkova EA, Aganov AV, Klochkov VV J Biomol NMR. 2015 Mar 19. PMID:25786621 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protegrin

Proteopedia Page Contributors and Editors (what is this?)

OCA