Cargando…
Functional Mapping of Human Dynamin-1-Like GTPase Domain Based on X-ray Structure Analyses
Human dynamin-1-like protein (DNM1L) is a GTP-driven molecular machine that segregates mitochondria and peroxisomes. To obtain insights into its catalytic mechanism, we determined crystal structures of a construct comprising the GTPase domain and the bundle signaling element (BSE) in the nucleotide-...
Autores principales: | Wenger, Julia, Klinglmayr, Eva, Fröhlich, Chris, Eibl, Clarissa, Gimeno, Ana, Hessenberger, Manuel, Puehringer, Sandra, Daumke, Oliver, Goettig, Peter |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3747075/ https://www.ncbi.nlm.nih.gov/pubmed/23977156 http://dx.doi.org/10.1371/journal.pone.0071835 |
Ejemplares similares
-
Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions
por: Eibl, Clarissa, et al.
Publicado: (2014) -
Structural and Functional
Analysis of the NLRP4 Pyrin
Domain
por: Eibl, Clarissa, et al.
Publicado: (2012) -
G domain dimerization controls dynamin's assembly-stimulated GTPase activity
por: Chappie, Joshua S., et al.
Publicado: (2010) -
Intrapolypeptide Interactions
between the GTPase Effector
Domain (GED) and the GTPase Domain Form the Bundle Signaling Element
in Dynamin Dimers
por: Srinivasan, Saipraveen, et al.
Publicado: (2014) -
Role of GTPase-Dependent Mitochondrial Dynamins in Heart Diseases
por: Liu, Jiangen, et al.
Publicado: (2021)