The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment

被引：67

作者：

Shishkov, AV

Goldanskii, VI

Baratova, LA

Fedorova, NV

Ksenofontov, AL

Zhirnov, OP

Galkin, AV ^{[1
]}

机构：

[1] Russian Acad Agr Sci, Inst Agr Biotechnol, Moscow 127550, Russia

[2] Russian Acad Sci, NN Semenov Chem Phys Inst, Moscow 117977, Russia

[3] Moscow MV Lomonosov State Univ, AN Belozersky Inst Physicochem Biol, Moscow 119899, Russia

[4] Russian Acad Med Sci, DI Ivanovsky Virol Inst, Moscow 123098, Russia

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 14期

关键词：

tritium planigraphy; three-dimensional modeling; topology; secondary structure prediction;

D O I：

10.1073/pnas.96.14.7827

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Intact influenza A virions were bombarded with thermally activated tritium atoms, and the intramolecular distribution of the label in the matrix protein M1 was analyzed to determine the in situ accessibility of its tryptic fragments. These data were combined with the previously reported x-ray crystal structure of the M1 fragment 2-158 [Sha, B, & Luo, M. (1997) Nat. Struct. Biol, 4, 239-244] and the predicted topology of the C domain (159-252) to propose a model of M1 arrangement in the virus particle.

引用

页码：7827 / 7830

页数：4

共 24 条

[1] Proteins on ribosome surface: Measurements of protein exposure by hot tritium bombardment technique [J].