The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment.
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.
Shishkov
A V
AV
N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow 117977, Russia.
Goldanskii
V I
VI
Baratova
L A
LA
Fedorova
N V
NV
Ksenofontov
A L
AL
Zhirnov
O P
OP
Galkin
A V
AV
D000818:Animals; D002642:Chick Embryo; D018360:Crystallography, X-Ray; D009980:Influenza A virus / Q000502:physiology* / Q000648:ultrastructure; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D014316:Tritium; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000302:isolation & purification
C031540:M-protein, influenza virus; C488936:M1 protein, Influenza A virus; D014763:Viral Matrix Proteins; D014316:Tritium