4ZV5

Crystal structure of N-myristoylated mouse mammary tumor virus matrix protein

4ZV5 の概要

• エントリーDOI: 10.2210/pdb4zv5/pdb
• 分子名称: Matrix protein p10, MYRISTIC ACID (3 entities in total)
• 機能のキーワード: retroviral matrix protein, n-myristoylation, viral protein
• 由来する生物種: Mouse mammary tumor virus (MMTV)
• 細胞内の位置: Matrix protein p10: Virion . Capsid protein p27: Virion . Nucleocapsid protein p14: Virion : P10258
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21434.85

構造登録者

Zabransky, A.,Dolezal, M.,Dostal, J.,Vanek, O.,Hadravova, R.,Stokrova, J.,Brynda, J.,Pichova, I. (登録日: 2015-05-18, 公開日: 2016-01-27, 最終更新日: 2024-11-13)

主引用文献

Dolezal, M.,Zabransky, A.,Dostal, J.,Vanek, O.,Brynda, J.,Lepsik, M.,Hadravova, R.,Pichova, I.
Myristoylation drives dimerization of matrix protein from mouse mammary tumor virus.
Retrovirology, 13:2-2, 2016

PubMed Abstract: Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the plasma membrane (PM) and is required for the assembly of most retroviruses. In betaretroviruses, which assemble immature particles in the cytoplasm, myristoylation is dispensable for assembly but is crucial for particle transport to the PM. Oligomerization of HIV-1 MA stimulates the transition of the myristoyl group from a sequestered to an exposed conformation, which is more accessible for membrane binding. However, for other retroviruses, the effect of MA oligomerization on myristoyl group exposure has not been thoroughly investigated.

PubMed: 26728401
DOI: 10.1186/s12977-015-0235-8

実験手法

X-RAY DIFFRACTION (1.57 Å)