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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| Vydáno v: | EMBO J |
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| Hlavní autoři: | , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Publishing Group
2002
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| Témata: | |
| On-line přístup: | 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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