Discovery of Allosteric Inhibition of Human ATP-Citrate Lyase

Name: Discovery of Allosteric Inhibition of Human ATP-Citrate Lyase
Creator: Granchi C.
Keywords: 0301 basic medicine, 0303 health sciences, 03 medical and health sciences, Adenosine Triphosphate, Multienzyme Complexes, ATP Citrate (pro-S)-Lyase, Humans, Oxo-Acid-Lyases, ACLY; cryo-electron microscopy; inhibitor; sulfonamide; X-ray structure, Lipid Metabolism

Granchi C.

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Article . 2019

Full-Text: https://arpi.unipi.it/request-item?handle=11568/991954&bitstreamId=e0d6c92d-7f1f-fcf8-e053-d805fe0aa794

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Trends in Pharmacological Sciences

Article . 2019 . Peer-reviewed

License: Elsevier TDM

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https://pubmed.ncbi.nlm.nih.go...

Article . 2020

Data sources: Europe PubMed Central

https://dx.doi.org/10.1016/j.t...

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Discovery of Allosteric Inhibition of Human ATP-Citrate Lyase

descriptionPublicationkeyboard_double_arrow_right Article 01 Jun 2019 Italy English Publisher:Elsevier BVJournal:Trends in Pharmacological Sciences, volume 40, pages 364-366 (issn: 0165-6147,

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Authors: Granchi C.;

doi: 10.1016/j.tips.2019.04.008

pmid: 31072639

handle: 11568/991954

Discovery of Allosteric Inhibition of Human ATP-Citrate Lyase

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Abstract

ATP-citrate lyase (ACLY) is an enzyme that links glycolysis to lipid metabolism. To date only partial X-ray structures of ACLY have been solved, thus limiting the design of novel inhibitors. Wei and colleagues (published online in Nature April 3, 2019) now report the full structure of human ACLY in complex with NDI-091143, revealing an appealing allosteric inhibition mechanism for this compound.

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Italy

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University of Pisa
Italy

Keywords

Adenosine Triphosphate, Multienzyme Complexes, ATP Citrate (pro-S)-Lyase, Humans, Oxo-Acid-Lyases, ACLY; cryo-electron microscopy; inhibitor; sulfonamide; X-ray structure, Lipid Metabolism

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