6HTL

Measles Phosphoprotein Coiled-Coil Domain IPKI Variant

6HTL の概要

• エントリーDOI: 10.2210/pdb6htl/pdb
• 分子名称: Phosphoprotein, CALCIUM ION (3 entities in total)
• 機能のキーワード: coiled-coil, alpha helix, tetramer, 3-10 helix, viral protein
• 由来する生物種: Measles morbillivirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8966.17

構造登録者

Schramm, A.,Longhi, S. (登録日: 2018-10-04, 公開日: 2019-06-05, 最終更新日: 2024-01-24)

主引用文献

Bloyet, L.M.,Schramm, A.,Lazert, C.,Raynal, B.,Hologne, M.,Walker, O.,Longhi, S.,Gerlier, D.
Regulation of measles virus gene expression by P protein coiled-coil properties.
Sci Adv, 5:eaaw3702-eaaw3702, 2019

PubMed Abstract: The polymerase of negative-stranded RNA viruses consists of the large protein (L) and the phosphoprotein (P), the latter serving both as a chaperon and a cofactor for L. We mapped within measles virus (MeV) P the regions responsible for binding and stabilizing L and showed that the coiled-coil multimerization domain (MD) of P is required for gene expression. MeV MD is kinked as a result of the presence of a stammer. Both restoration of the heptad regularity and displacement of the stammer strongly decrease or abrogate activity in a minigenome assay. By contrast, P activity is rather tolerant of substitutions within the stammer. Single substitutions at the "a" or "d" hydrophobic anchor positions with residues of variable hydrophobicity revealed that P functionality requires a narrow range of cohesiveness of its MD. Results collectively indicate that, beyond merely ensuring P oligomerization, the MD finely tunes viral gene expression through its cohesiveness.

PubMed: 31086822
DOI: 10.1126/sciadv.aaw3702

実験手法

X-RAY DIFFRACTION (2.3 Å)