Article

Cryo-EM analysis of human mitochondrial Hsp90 in multiple tetrameric states

2020-11-04

Abstract excerpt

Hsp90 is a ubiquitous molecular chaperone that mediates the folding and maturation of hundreds of “client” proteins. Although Hsp90s generally function as homodimers, recent discoveries suggested that the mitochondrion specific Hsp90 (TRAP1) also forms functionally relevant tetramers. The structural mechanism of tetramer formation remains elusive. Here we used a combination of solution, biochemical and cryo-electr...

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Literature Corpus work: 2fbaf508-1604-5a92-a100-d9827f336355
DOI: 10.1101/2020.11.04.368837

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