2F76

Solution structure of the M-PMV wild type matrix protein (p10)

2F76 の概要

• エントリーDOI: 10.2210/pdb2f76/pdb
• 関連するPDBエントリー: 2F77
• NMR情報: BMRB: 6400
• 分子名称: Core protein p10 (1 entity in total)
• 機能のキーワード: 4 alpha-helices, viral protein
• 由来する生物種: Simian retrovirus 1
• 細胞内の位置: Matrix protein p10: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p14: Virion (Potential): P04022
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11985.78

構造登録者

Vlach, J.,Lipov, J.,Veverka, V.,Lang, J.,Srb, P.,Rumlova, M.,Hunter, E.,Ruml, T.,Hrabal, R. (登録日: 2005-11-30, 公開日: 2006-12-05, 最終更新日: 2024-05-29)

主引用文献

Vlach, J.,Lipov, J.,Rumlova, M.,Veverka, V.,Lang, J.,Srb, P.,Knejzlik, Z.,Pichova, I.,Hunter, E.,Hrabal, R.,Ruml, T.
D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.
Proc.Natl.Acad.Sci.USA, 105:10565-10570, 2008

PubMed Abstract: Despite extensive data demonstrating that immature retroviral particle assembly can take place either at the plasma membrane or at a distinct location within the cytoplasm, targeting of viral precursor proteins to either assembly site still remains poorly understood. Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site. Comparison of the three-dimensional structures of M-PMV wild-type matrix protein (wt MA) with a single amino acid mutant (R55F), which redirects assembly from a cytoplasmic site to the plasma membrane, revealed different mutual orientations of their C- and N-terminal domains. This conformational change buries a putative intracellular targeting motif located between both domains in the hydrophobic pocket of the MA molecule, thereby preventing the interaction with cellular transport mechanisms.

PubMed: 18647839
DOI: 10.1073/pnas.0801765105

実験手法

SOLUTION NMR