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Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
Biebl, Maximilian M; Lopez, Abraham; Rehn, Alexandra; Freiburger, Lee; Lawatscheck, Jannis; Blank, Birgit; Sattler, Michael; Buchner, Johannes.
Affiliation
  • Biebl MM; Department of Chemistry, Technische Universität München, Garching, Germany.
  • Lopez A; Department of Chemistry, Technische Universität München, Garching, Germany.
  • Rehn A; Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany.
  • Freiburger L; Department of Chemistry, Technische Universität München, Garching, Germany.
  • Lawatscheck J; Institut für Mikrobiologie der Bundeswehr, München, Germany.
  • Blank B; Department of Chemistry, Technische Universität München, Garching, Germany.
  • Sattler M; Zymeworks Inc., Vancouver, BC, Canada.
  • Buchner J; Department of Chemistry, Technische Universität München, Garching, Germany.
Nat Commun ; 12(1): 828, 2021 02 05.
Article in En | MEDLINE | ID: mdl-33547294
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Receptors, Glucocorticoid / Adenylyl Imidodiphosphate / Molecular Chaperones / HSP90 Heat-Shock Proteins / Saccharomyces cerevisiae Proteins / Prostaglandin-E Synthases Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2021 Document type: Article Affiliation country: Country of publication:
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Receptors, Glucocorticoid / Adenylyl Imidodiphosphate / Molecular Chaperones / HSP90 Heat-Shock Proteins / Saccharomyces cerevisiae Proteins / Prostaglandin-E Synthases Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2021 Document type: Article Affiliation country: Country of publication: