Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase

Chloe R. Koulouris; Sian E. Gardiner; Tessa K. Harris; Karen T. Elvers; S. Mark Roe; Jason A. Gillespie; Simon E. Ward; Olivera Grubisha; Robert A. Nicholls; John R. Atack; Benjamin D. Bax

doi:10.1038/s42003-022-03264-5

Communications Biology (Apr 2022)

Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase

Chloe R. Koulouris,
Sian E. Gardiner,
Tessa K. Harris,
Karen T. Elvers,
S. Mark Roe,
Jason A. Gillespie,
Simon E. Ward,
Olivera Grubisha,
Robert A. Nicholls,
John R. Atack,
Benjamin D. Bax

Affiliations

Chloe R. Koulouris: Sussex Drug Discovery Centre, University of Sussex
Sian E. Gardiner: Medicines Discovery Institute, Cardiff University
Tessa K. Harris: Medicines Discovery Institute, Cardiff University
Karen T. Elvers: Medicines Discovery Institute, Cardiff University
S. Mark Roe: Department of Biochemistry and Biomedicine, University of Sussex
Jason A. Gillespie: Medicines Discovery Institute, Cardiff University
Simon E. Ward: Medicines Discovery Institute, Cardiff University
Olivera Grubisha: Medicines Discovery Institute, Cardiff University
Robert A. Nicholls: MRC Laboratory of Molecular Biology
John R. Atack: Medicines Discovery Institute, Cardiff University
Benjamin D. Bax: Medicines Discovery Institute, Cardiff University

DOI: https://doi.org/10.1038/s42003-022-03264-5
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 15

Abstract

Read online

The catalytic mechanisms of human serine racemase reveal a ligandable pocket near Tyr121 that could be targeted for the development of novel inhibitors.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

About the journal