Conformational changes in tubulin upon binding cryptophycin-52 reveal its mechanism of action.

Eren, Elif; Watts, Norman R; Sackett, Dan L; Wingfield, Paul T

Eren, Elif; Watts, Norman R; Sackett, Dan L; Wingfield, Paul T.

Affiliation

Eren E; Protein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, Maryland, USA.
Watts NR; Protein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, Maryland, USA.
Sackett DL; Division of Basic and Translational Biophysics, NICHD, National Institutes of Health, Bethesda, Maryland, USA.
Wingfield PT; Protein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, Maryland, USA. Electronic address: wingfiep@mail.nih.gov.

J Biol Chem ; 297(4): 101138, 2021 10.

Article in En | MEDLINE | ID: mdl-34461087

Subject(s)

Depsipeptides/chemistry; Lactams/chemistry; Lactones/chemistry; Tubulin/chemistry; Cryoelectron Microscopy; Depsipeptides/pharmacology; HeLa Cells; Humans; Lactams/pharmacology; Lactones/pharmacology; Protein Domains

Key words

LY355703; anticancer drug; conformational change; cryo-EM; cryptophycin-1; cryptophycin-52; cyclodepsipeptide; maytansine site; microtubule; tubulin

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Tubulin / Depsipeptides / Lactams / Lactones Limits: Humans Language: En Journal: J Biol Chem Year: 2021 Type: Article Affiliation country: United States

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