Structure of the helicase core of Werner helicase, a key target in microsatellite instability cancers.


Journal

Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869

Informations de publication

Date de publication:
01 2021
Historique:
received: 26 05 2020
revised: 28 10 2020
accepted: 28 10 2020
entrez: 17 11 2020
pubmed: 18 11 2020
medline: 15 9 2021
Statut: epublish

Résumé

Loss of WRN, a DNA repair helicase, was identified as a strong vulnerability of microsatellite instable (MSI) cancers, making WRN a promising drug target. We show that ATP binding and hydrolysis are required for genome integrity and viability of MSI cancer cells. We report a 2.2-Å crystal structure of the WRN helicase core (517-1,093), comprising the two helicase subdomains and winged helix domain but not the HRDC domain or nuclease domains. The structure highlights unusual features. First, an atypical mode of nucleotide binding that results in unusual relative positioning of the two helicase subdomains. Second, an additional β-hairpin in the second helicase subdomain and an unusual helical hairpin in the Zn

Identifiants

pubmed: 33199508
pii: 4/1/e202000795
doi: 10.26508/lsa.202000795
pmc: PMC7671478
pii:
doi:

Substances chimiques

Cell Cycle Proteins 0
Proto-Oncogene Proteins 0
Adenosine Diphosphate 61D2G4IYVH
Adenosine Triphosphate 8L70Q75FXE
DNA 9007-49-2
Protein Serine-Threonine Kinases EC 2.7.11.1
WRN protein, human EC 3.6.4.12
Werner Syndrome Helicase EC 3.6.4.12
Zinc J41CSQ7QDS

Banques de données

PDB
['2WWY', '3AAF', '6YHR']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 106169/ZZ14/Z
Pays : United Kingdom

Informations de copyright

© 2020 Newman et al.

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Auteurs

Joseph A Newman (JA)

Structural Genomics Consortium, University of Oxford, Oxford, UK.

Angeline E Gavard (AE)

Structural Genomics Consortium, University of Oxford, Oxford, UK.

Simone Lieb (S)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Madhwesh C Ravichandran (MC)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Katja Hauer (K)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Patrick Werni (P)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Leonhard Geist (L)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Jark Böttcher (J)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

John R Engen (JR)

Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.

Klaus Rumpel (K)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Matthias Samwer (M)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Mark Petronczki (M)

Boehringer Ingelheim RCV GmbH & Co KG, Vienna, Austria.

Opher Gileadi (O)

Structural Genomics Consortium, University of Oxford, Oxford, UK opher.gileadi@cmd.ox.ac.uk.

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Classifications MeSH