Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain

The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 Å reso...

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Autors principals: Jogl, Gerwald, Shen, Yang, Gebauer, Damara, Li, Jiang, Wiegmann, Katja, Kashkar, Hamid, Krönke, Martin, Tong, Liang
Format: Article
Idioma:en
Publicat: Oxford University Press 2002
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC126298/
https://ncbi.nlm.nih.gov/pubmed/12234919
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/cdf502
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https://ncbi.nlm.nih.gov/pmc/articles/PMC126298/
https://ncbi.nlm.nih.gov/pubmed/12234919
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/cdf502

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