Linked Life Data

21166595

Source:http://linkedlifedata.com/resource/pubmed/id/21166595

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-1-13
pubmed:abstractText
The human myxovirus resistance protein 1 (MxA) is a key mediator of the interferon-induced antiviral response against a wide range of viruses. MxA expression is tightly regulated by type I and type III interferons, requires signal transducer and activator of transcription 1 signaling, and is not inducible directly by viruses or other stimuli. MxA shares many properties with the dynamin superfamily of large GTPases. It consists of 3 domains, namely, an N-terminal GTPase domain that binds and hydrolyses GTP, a middle domain mediating self-assembly, and a carboxy-terminal GTPase effector domain. Like dynamin, MxA has the ability to self-assemble into highly ordered oligomers and to form ring-like structures around liposomes, inducing liposome tubulation. The structural details of MxA oligomerization have recently been elucidated, providing new insights into the antiviral mechanism of this mechanochemical enzyme. The structural and functional data suggest that MxA targets the nucleoprotein of MxA-sensitive viruses. Thus, MxA may form oligomeric rings around tubular nucleocapsid structures, thereby inhibiting their transcriptional and replicative function. Here we briefly review the most salient features of MxA expression and antiviral function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1557-7465
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-87
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity.
pubmed:affiliation
Department of Virology, Institute of Medical Microbiology and Hygiene, University of Freiburg, Freiburg, Germany. otto.haller@uniklinik-freiburg.de
pubmed:publicationType
Journal Article, Review