1BAX

MASON-PFIZER MONKEY VIRUS MATRIX PROTEIN, NMR, AVERAGE STRUCTURE

「1AT7」から置き換えられました

1BAX の概要

• エントリーDOI: 10.2210/pdb1bax/pdb
• 分子名称: M-PMV MATRIX PROTEIN (1 entity in total)
• 機能のキーワード: matrix protein, core protein, polyprotein, myristylation
• 由来する生物種: Mason-Pfizer monkey virus
• 細胞内の位置: Matrix protein p10: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p14: Virion (Potential): P07567
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11316.98

構造登録者

Conte, M.R.,Klikova, M.,Hunter, E.,Ruml, T.,Matthews, S. (登録日: 1998-04-20, 公開日: 1998-06-17, 最終更新日: 2024-04-10)

主引用文献

Conte, M.R.,Klikova, M.,Hunter, E.,Ruml, T.,Matthews, S.
The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly.
EMBO J., 16:5819-5826, 1997

PubMed Abstract: The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D retroviruses. In type B and D retroviruses, the Gag protein pre-assembles before association with the membrane, whereas in type C retroviruses (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma membrane, where the particle formation occurs. The N-terminal domain of Gag, the matrix protein (MA), plays a critical role in determining this morphogenic difference. We have determined the three-dimensional solution structure of the M-PMV MA by heteronuclear nuclear magnetic resonance. The protein contains four alpha-helices that are structurally similar to the known type C MA structures. This similarity implies possible common assembly units and membrane-binding mechanisms for type C and B/D retroviruses. In addition to this, the interpretation of mutagenesis data has enabled us to identify, for the first time, the structural basis of a putative intracellular targeting motif.

PubMed: 9312040
DOI: 10.1093/emboj/16.19.5819

実験手法

SOLUTION NMR