EMD-10575
PKM2 in complex with Compound 5
EMD-10575
Single-particle3.2 Å
Deposition: 27/12/2019Map released: 15/01/2020
Last modified: 22/05/2024
Sample Organism:
Homo sapiens
Sample: Pyruvate Kinase M2
Fitted models: 6ttf (Avg. Q-score: 0.548)
Raw data: EMPIAR-10648
Deposition Authors: Saur M
,
Hartshorn MJ
Sample: Pyruvate Kinase M2
Fitted models: 6ttf (Avg. Q-score: 0.548)
Raw data: EMPIAR-10648
Deposition Authors: Saur M
,
Hartshorn MJ
Fragment-based drug discovery using cryo-EM.
Saur M ,
Hartshorn MJ,
Dong J,
Reeks J,
Bunkoczi G,
Jhoti H,
Williams PA
(2020) Drug Discov Today , 25 , 485 - 490
,
Hartshorn MJ,
Dong J,
Reeks J,
Bunkoczi G,
Jhoti H,
Williams PA
(2020) Drug Discov Today , 25 , 485 - 490
Abstract:
Recent advances in electron cryo-microscopy (cryo-EM) structure determination have pushed the resolutions obtainable by the method into the range widely considered to be of utility for drug discovery. Here, we review the use of cryo-EM in fragment-based drug discovery (FBDD) based on in-house method development. We demonstrate not only that cryo-EM can reveal details of the molecular interactions between fragments and a protein, but also that the current reproducibility, quality, and throughput are compatible with FBDD. We exemplify this using the test system β-galactosidase (Bgal) and the oncology target pyruvate kinase 2 (PKM2).
Recent advances in electron cryo-microscopy (cryo-EM) structure determination have pushed the resolutions obtainable by the method into the range widely considered to be of utility for drug discovery. Here, we review the use of cryo-EM in fragment-based drug discovery (FBDD) based on in-house method development. We demonstrate not only that cryo-EM can reveal details of the molecular interactions between fragments and a protein, but also that the current reproducibility, quality, and throughput are compatible with FBDD. We exemplify this using the test system β-galactosidase (Bgal) and the oncology target pyruvate kinase 2 (PKM2).