Structural polymorphism in F-actin View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2010-11

AUTHORS

Vitold E Galkin, Albina Orlova, Gunnar F Schröder, Edward H Egelman

ABSTRACT

Actin has maintained an exquisite degree of sequence conservation over large evolutionary distances for reasons that are not understood. The desire to explain phenomena from muscle contraction to cytokinesis in mechanistic detail has driven the generation of an atomic model of the actin filament (F-actin). Here we use electron cryomicroscopy to show that frozen-hydrated actin filaments contain a multiplicity of different structural states. We show (at ∼10 Å resolution) that subdomain 2 can be disordered and can make multiple contacts with the C terminus of a subunit above it. We link a number of disease-causing mutations in the human ACTA1 gene to the most structurally dynamic elements of actin. Because F-actin is structurally polymorphic, it cannot be described using only one atomic model and must be understood as an ensemble of different states. More... »

PAGES

1318

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.1930

DOI

http://dx.doi.org/10.1038/nsmb.1930

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041943227

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20935633


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Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

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N-Triples is a line-based linked data format ideal for batch operations.

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Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/nsmb.1930'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/nsmb.1930'


 

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