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@ARTICLE{Gao:18855,
author = {Gao, S and von der Malsburg, A. and Dick, A. and Faelber,
K. and Schröder, G.F. and Haller, O. and Kochs, G. and
Daumke, O.},
title = {{S}tructure of {M}yxovirus {R}esistance {P}rotein {A}
{R}eveals {I}ntra- and {I}ntermolecular {D}omain
{I}nteractions {R}equired for the {A}ntiviral {F}unction},
journal = {Immunity},
volume = {35},
issn = {1074-7613},
address = {[Cambridge, Mass.]},
publisher = {Cell Press},
reportid = {PreJuSER-18855},
pages = {514 - 525},
year = {2011},
note = {This project was supported by grants of the Deutsche
Forschungsgemeinschaft (SFB 740/TP C7 and SFB958/A12 to O.D.
and Ko1579/8-1 to G.K.), by a Career Development Fellowship
of The International Human Frontier Science Program
Organization, and by the EMBO Young Investigator Program to
O.D. We are grateful to A. Brunger for providing us with the
prerelease of CNS version 1.3, the BESSY staff at beamline
BL14.1 and SLS staff at beamline X06SA for help with data
collection, and S. Werner, S. Paeschke, and S. Gruber for
technical assistance.},
abstract = {Human myxovirus resistance protein 1 (MxA) is an
interferon-induced dynamin-like GTPase that acts as a
cell-autonomous host restriction factor against many viral
pathogens including influenza viruses. To study the
molecular principles of its antiviral activity, we
determined the crystal structure of nucleotide-free MxA,
which showed an extended three-domain architecture. The
central bundle signaling element (BSE) connected the
amino-terminal GTPase domain with the stalk via two hinge
regions. MxA oligomerized in the crystal via the stalk and
the BSE, which in turn interacted with the stalk of
the neighboring monomer. We demonstrated that the intra-
and intermolecular domain interplay between the BSE and
stalk was essential for oligomerization and the antiviral
function of MxA. Based on these results, we propose a
structural model for the mechano-chemical coupling in
ring-like MxA oligomers as the principle mechanism for this
unique antiviral effector protein.},
keywords = {Animals / Cell Line / Crystallography, X-Ray / GTP-Binding
Proteins: chemistry / Humans / Models, Molecular / Protein
Structure, Quaternary / Protein Structure, Tertiary /
Structural Homology, Protein / myxovirus resistance proteins
(NLM Chemicals) / GTP-Binding Proteins (NLM Chemicals) / J
(WoSType)},
cin = {ICS-6},
ddc = {610},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {Funktion und Dysfunktion des Nervensystems / BioSoft:
Makromolekulare Systeme und biologische
Informationsverarbeitung},
pid = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
shelfmark = {Immunology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21962493},
UT = {WOS:000296657700011},
doi = {10.1016/j.immuni.2011.07.012},
url = {https://juser.fz-juelich.de/record/18855},
}