5cgn | pdb_00005cgn

Structure of quasiracemic Ala-Magainin 2 with a beta amino acid substitution at position 8

spinqualitylabelsall models 5cgn, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cgn is a 8 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, DAL, DGL, DHI, DIL, DLE, DLY, DPN, DSE, DSG, DVA, MED, XCP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MAGA_XENLA Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents. Publication Abstract from PubMed Quasiracemic crystallography has been used to explore the significance of homochiral and heterochiral associations in a set of host-defense peptide derivatives. The previously reported racemic crystal structure of a magainin 2 derivative displayed a homochiral antiparallel dimer association featuring a "phenylalanine zipper" notable for the dual roles of phenylalanines in mediating dimerization and formation of an exposed hydrophobic swath. This motif is seen as well in two new quasiracemate crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a beta-amino acid residue. This structural trend supports the hypothesis that the Phe zipper motif has functional significance. Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif.,Hayouka Z, Thomas NC, Mortenson DE, Satyshur KA, Weisblum B, Forest KT, Gellman SH J Am Chem Soc. 2015 Sep 23;137(37):11884-7. doi: 10.1021/jacs.5b07206. Epub 2015 , Sep 10. PMID:26369301 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Magainin 2

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