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Crystal Structure of Sphingosine Kinase 1 with PF-543

DOI: 10.1021/ml5004074 DOI Help
PMID: 25516793 PMID Help

Authors: Jing Wang (University of Oxford) , Stefan Knapp (Structural Genomics Consortium, University of Oxford) , Nigel J. Pyne (University of Strathclyde) , Susan Pyne (University of Strathclyde) , Jonathan M. Elkins (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acs Medicinal Chemistry Letters , VOL 5 (12) , PAGES 1329 - 1333

State: Published (Approved)
Published: December 2014
Diamond Proposal Number(s): 8421 , 10619

Open Access Open Access

Abstract: The most potent inhibitor of Sphingosine Kinase 1 (SPHK1) so far identified is PF-543. The crystal structure of SPHK1 in complex with inhibitor PF-543 to 1.8 Å resolution reveals the inhibitor bound in a bent conformation analogous to that expected of a bound sphingosine substrate but with a rotated head group. The structural data presented will aid in the design of SPHK1 and SPHK2 inhibitors with improved properties.

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I02-Macromolecular Crystallography