Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM
Copyright policy )Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM
Cryo-EM reveals the remodeling of RUVBL1-RUVBL2 ATPases by the client recruitment component in the HSP90 co-chaperone R2TP.
- Instituto de Salud Carlos III Spain
- Spanish National Cancer Research Centre Spain
- University of Sussex United Kingdom
Models, Molecular, Protein Conformation, alpha-Helical, Adenosine Triphosphate, DOMAIN, Protein Domains, BINDING, HSP90, Humans, TEL2, Histidine, HSP90 Heat-Shock Proteins, Research Articles, QP0601, COMPLEX, Binding Sites, QP0501, Nucleotides, MTOR, Cryoelectron Microscopy, DNA Helicases, Adenosine Diphosphate, COCHAPERONE, Multiprotein Complexes, ATPases Associated with Diverse Cellular Activities, Apoptosis Regulatory Proteins, Carrier Proteins, Protein Binding
Models, Molecular, Protein Conformation, alpha-Helical, Adenosine Triphosphate, DOMAIN, Protein Domains, BINDING, HSP90, Humans, TEL2, Histidine, HSP90 Heat-Shock Proteins, Research Articles, QP0601, COMPLEX, Binding Sites, QP0501, Nucleotides, MTOR, Cryoelectron Microscopy, DNA Helicases, Adenosine Diphosphate, COCHAPERONE, Multiprotein Complexes, ATPases Associated with Diverse Cellular Activities, Apoptosis Regulatory Proteins, Carrier Proteins, Protein Binding
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