2VQP

Structure of the matrix protein from human Respiratory Syncytial Virus

2VQP の概要

• エントリーDOI: 10.2210/pdb2vqp/pdb
• 分子名称: MATRIX PROTEIN, GLYCEROL, FORMIC ACID, ... (5 entities in total)
• 機能のキーワード: viral protein, viral matrix protein, peripheral membrane protein, rsv, virion, matrix protein, envelope protein
• 由来する生物種: HUMAN RESPIRATORY SYNCYTIAL VIRUS
• 細胞内の位置: Virion: P03419
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29570.99

構造登録者

Money, V.A.,McPhee, H.K.,Sanderson, J.M.,Yeo, R.P. (登録日: 2008-03-18, 公開日: 2009-02-17, 最終更新日: 2024-05-08)

主引用文献

Money, V.A.,Mcphee, H.K.,Mosely, J.A.,Sanderson, J.M.,Yeo, R.P.
Surface Features of a Mononegavirales Matrix Protein Indicate Sites of Membrane Interaction.
Proc.Natl.Acad.Sci.USA, 106:4441-, 2009

PubMed Abstract: The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has been crystallized and the structure determined to a resolution of 1.6 A. The structure comprises 2 compact beta-rich domains connected by a relatively unstructured linker region. Due to the high degree of side-chain order in the structure, an extensive contiguous area of positive surface charge covering approximately 600 A(2) can be resolved. This unusually large patch of positive surface potential spans both domains and the linker, and provides a mechanism for driving the interaction of the protein with a negatively-charged membrane surface or other virion components such as the nucleocapsid. This patch is complemented by regions of high hydrophobicity and a striking planar arrangement of tyrosine residues encircling the C-terminal domain. Comparison of the RSV M sequence with other members of the Pneumovirinae shows that regions of divergence correspond to surface exposed loops in the M structure, with the majority of viral species-specific differences occurring in the N-terminal domain.

PubMed: 19251668
DOI: 10.1073/PNAS.0805740106

実験手法

X-RAY DIFFRACTION (1.6 Å)