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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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Bibliografiska uppgifter
Huvudupphovsmän: Niemann, Hartmut H., Knetsch, Menno L.W., Scherer, Anna, Manstein, Dietmar J., Kull, F.Jon
Materialtyp: Artigo
Språk:Inglês
Publicerad: Oxford University Press 2001
Ämnen:
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC125706/
https://ncbi.nlm.nih.gov/pubmed/11689422
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/20.21.5813
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