Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation
2013; American Association for the Advancement of Science; Volume: 340; Issue: 6139 Linguagem: Inglês
10.1126/science.1237908
ISSN1095-9203
AutoresJean-François Trempe, Véronique Sauvé, Karl Grenier, Marjan Seirafi, Matthew Y. H. Tang, Marie Ménade, M. Sameer Al‐Abdul‐Wahid, Jonathan D. Krett, Kathy Wong, Guennadi Kozlov, Bhushan Nagar, Edward A. Fon, Kalle Gehring,
Tópico(s)Click Chemistry and Applications
ResumoParkin Enhanced? Inactivation of parkin, an E3 ubiquitin ligase, is responsible for a familial form of Parkinson's disease and may be involved in sporadic forms as well. Trempe et al. (p. 1451 , published online 9 May) present the crystal structure of full-length parkin in an autoinhibited configuration. Guided by the structure, mutations were designed that activated parkin both in vitro and in cells. Because parkin is neuroprotective, the structure provides a framework for enhancing parkin function as a therapeutic strategy in Parkinson's disease.
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