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The BECN1 coiled coil domain: An “imperfect” homodimer interface that facilitates ATG14 and UVRAG binding
The coiled-coil domain of BECN1 serves as a protein interaction platform to recruit two major autophagy regulators ATG14 and UVRAG. Our crystal structure of the BECN1 coiled-coil domain reveals a homodimer with an imperfect dimer interface. This “imperfect” feature favors the formation of a stable B...
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| Auteurs principaux: | , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
Landes Bioscience
2012
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3679240/ https://ncbi.nlm.nih.gov/pubmed/22647755 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.4161/auto.20750 |
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