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-...
Enregistré dans:
Auteurs principaux: | Julia Wenger, Eva Klinglmayr, Chris Fröhlich, Clarissa Eibl, Ana Gimeno, Manuel Hessenberger, Sandra Puehringer, Oliver Daumke, Peter Goettig |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Public Library of Science (PLoS)
2013
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/6e3cec825e404f56a4b6e73fabce42dc |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly.
par: Swagata Chakraborty, et autres
Publié: (2012) -
Small GTPases and BAR domain proteins regulate branched actin polymerisation for clathrin and dynamin-independent endocytosis
par: Mugdha Sathe, et autres
Publié: (2018) -
Publisher Correction: Small GTPases and BAR domain proteins regulate branched actin polymerisation for clathrin and dynamin-independent endocytosis
par: Mugdha Sathe, et autres
Publié: (2021) -
A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling
par: Sho W Suzuki, et autres
Publié: (2021) -
p190RhoGAP proteins contain pseudoGTPase domains
par: Amy L. Stiegler, et autres
Publié: (2017)