Supplemental Material Fine-tuning of the Hsc70-based human protein disaggregase machinery by the distinctive C-terminal extension of Apg2

8 pages. -- Table 1. SAXS data collection and processing. -- Figure S1: Binding of nucleotides does not promote significant conformational changes in Apg2 and Apg2C tertiary structure. -- Figure S2: Characterization of the interaction of Apg2ΔC with Hsc70 in the absence of nucleotides by SPR. -- Fi...

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Detalles Bibliográficos
Autores: Cabrera, Yovana, Bernardo-Seisdedos, Ganeko, Dublang, Leire, Albesa-Jové, David, Orozco, Natalia, Viguera, Ana Rosa, Millet, Óscar, Muga, Arturo, Moro, Fernando
Tipo de recurso: conjunto de datos
Fecha de publicación:2022
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/331446
Acceso en línea:http://hdl.handle.net/10261/331446
Access Level:acceso abierto
Descripción
Sumario:8 pages. -- Table 1. SAXS data collection and processing. -- Figure S1: Binding of nucleotides does not promote significant conformational changes in Apg2 and Apg2C tertiary structure. -- Figure S2: Characterization of the interaction of Apg2ΔC with Hsc70 in the absence of nucleotides by SPR. -- Fig. S3: NMR chemical shift perturbation analysis. -- Fig- S4: Apg2IDR interacts with Hsc70 with 2-fold reduced affinity in the presence of nucleotides.

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