5CGO

Structure of quasiracemic Ala-Magainin 2 with a beta amino acid substitution at position 13

5CGO の概要

• エントリーDOI: 10.2210/pdb5cgo/pdb
• 関連するPDBエントリー: 4MGP 5CGN
• 分子名称: ACPC-13 derivative of Ala-Magainin 2, D-Ala-Magainin 2 (3 entities in total)
• 機能のキーワード: antimicrobial, quasiracemate, homochiral dimerization, beta amino acids, antimicrobial protein
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 10036.08

構造登録者

Hayouka, Z.,Thomas, N.C.,Mortenson, D.E.,Satyshur, K.A.,Weisblum, B.,Forest, K.T.,Gellman, S.H. (登録日: 2015-07-09, 公開日: 2015-09-23, 最終更新日: 2023-11-15)

主引用文献

Hayouka, Z.,Thomas, N.C.,Mortenson, D.E.,Satyshur, K.A.,Weisblum, B.,Forest, K.T.,Gellman, S.H.
Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif.
J.Am.Chem.Soc., 137:11884-11887, 2015

PubMed Abstract: 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crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue. This structural trend supports the hypothesis that the Phe zipper motif has functional significance.

PubMed: 26369301
DOI: 10.1021/jacs.5b07206

実験手法

X-RAY DIFFRACTION (1.5 Å)