Acta Crystallographica Section F Structural Biology and Crystallization Communications · 2009 · 13 citations · 16 references
Life SciencesBiochemistryMolecular BiologyEnzymologyNeurodegenerationStructural BiologyHuntington DiseaseNeurodegenerative DiseasesProtein DegradationProtein DomainsProtein Interaction DomainsProtein StructureDomain - Domain InteractionsDomain-domain InteractionsDomain-protein InteractionsE2 Ubiquitin-conjugating EnzymesHuntingtin ProteinProtein Domain OrganizationUbiquitin SystemUbiquitin-binding Domains
The ubiquitin-conjugating enzyme E2-25K has been identified as a huntingtin (the key protein in Huntington's disease) interacting protein and has been shown to play a role in mediating the toxicity of Abeta, the principal protein involved in Alzheimer's disease pathogenesis. E2-25K is a dual-domain protein with an ubiquitin-associated (UBA) domain as well as a conserved ubiquitin-conjugating (UBC) domain which catalyzes the formation of a covalent bond between the C-terminal glycine of an ubiquitin molecule and the -amine of a lysine residue on the acceptor protein as part of the ubiquitin-proteasome pathway. The crystal structures of E2-25K M172A mutant protein at pH 6.5 and pH 8.5 were determined to 1.9 and 2.2 A resolution, respectively. Examination of the structures revealed domain-domain interactions between the UBC and UBA domains which have not previously been reported.
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The PyMOL Molecular Graphics System
Warren L. DeLano · Medical Entomology and Zoology · 2002 · 18.1K citations