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The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes

Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human dynamin-1. Chemical modification of two cysteine residues, positioned in the middle domain and GTPas...

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Udgivet i:EMBO J
Principais autores: Klockow, Boris, Tichelaar, Willem, Madden, Dean R., Niemann, Hartmut H., Akiba, Toshihiko, Hirose, Keiko, Manstein, Dietmar J.
Format: Artigo
Sprog:Inglês
Udgivet: Nature Publishing Group 2002
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Article
Online adgang:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC125838/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11823417/
https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/21.3.240
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