5cgo
Structure of quasiracemic Ala-Magainin 2 with a beta amino acid substitution at position 13Structure of quasiracemic Ala-Magainin 2 with a beta amino acid substitution at position 13
Structural highlights
FunctionMAGA_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 PubMedQuasiracemic 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crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a beta-amino acid residue.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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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