Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 Å crystal structure of the nucleoti...

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Bibliografski detalji

Izdano u:	EMBO J
Glavni autori:	Niemann, Hartmut H., Knetsch, Menno L.W., Scherer, Anna, Manstein, Dietmar J., Kull, F.Jon
Format:	Artigo
Jezik:	Inglês
Izdano:	Nature Publishing Group 2001
Teme:	Article
Online pristup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC125706/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11689422/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/20.21.5813
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