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Crystal Structure of Sphingosine Kinase 1 with PF-543

descriptionPublicationkeyboard_double_arrow_right Article 31 Oct 2014 United Kingdom English Publisher:American Chemical Society (ACS)Journal:ACS Medicinal Chemistry Letters, volume 5, pages 1,329-1,333 (issn: 1948-5875, eissn: 1948-5875, Copyright policy )
Authors: Wang, Jing; Knapp, Stefan; Pyne, Nigel J.; Pyne, Susan; Elkins, Jonathan M.;

doi: 10.1021/ml5004074

pmid: 25516793

pmc: PMC4265818

Crystal Structure of Sphingosine Kinase 1 with PF-543

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.

Country
United Kingdom
Related Organizations
Keywords

570, Pharmacy and materia medica, 540, RS

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
95
Top 10%
Top 10%
Top 10%
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