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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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| Hauptverfasser: | , , , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Oxford University Press
2002
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC125838/ https://ncbi.nlm.nih.gov/pubmed/11823417 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/21.3.240 |
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