5EH4

Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase

5EH4 の概要

• エントリーDOI: 10.2210/pdb5eh4/pdb
• 関連するPDBエントリー: 5EH6
• 分子名称: Glycophorin-A, (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (2 entities in total)
• 機能のキーワード: receptor, lipidic cubic phase, peptides, transmembrane, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 13524.76

構造登録者

Call, M.J.,Call, M.E.,Trenker, R. (登録日: 2015-10-28, 公開日: 2015-12-23, 最終更新日: 2023-09-27)

主引用文献

Trenker, R.,Call, M.E.,Call, M.J.
Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase.
J.Am.Chem.Soc., 137:15676-15679, 2015

PubMed Abstract: The mechanisms of assembly and function for many important type I/II (single-pass) transmembrane (TM) receptors are proposed to involve the formation and/or alteration of specific interfaces among their membrane-embedded α-helical TM domains. The application of lipidic cubic phase (LCP) bilayer media for crystallization of single-α-helical TM complexes has the potential to provide valuable structural and mechanistic insights into many such systems. However, the fidelity of the interfaces observed in crowded crystalline arrays has been difficult to establish from the very limited number of such structures determined using X-ray diffraction data. Here we examine this issue using the glycophorin A (GpA) model system, whose homodimeric TM helix interface has been characterized by solution and solid-state NMR and biochemical techniques but never crystallographically. We report that a GpA-TM peptide readily crystallized in a monoolein cubic phase bilayer, yielding a dimeric α-helical structure that is in excellent agreement with previously reported NMR measurements made in several different types of host media. These results provide compelling support for the wider application of LCP techniques to enable X-ray crystallographic analysis of single-pass TM interactions.

PubMed: 26642914
DOI: 10.1021/jacs.5b11354

実験手法

X-RAY DIFFRACTION (2.81 Å)