3vzd: Difference between revisions

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==About this Structure==
==About this Structure==
[[3vzd]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZD OCA].  
[[3vzd]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZD OCA].  


==Reference==
==Reference==
<references group="xtra"/><references/>
<ref group="xtra">PMID:023602659</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Sphinganine kinase]]
[[Category: Sphinganine kinase]]
[[Category: Min, X.]]
[[Category: Min, X.]]

Revision as of 05:53, 29 January 2014

Template:STRUCTURE 3vzd

Crystal structure of Sphingosine Kinase 1 with inhibitor and ADP

Template:ABSTRACT PUBMED 23602659

Function

[SPHK1_HUMAN] Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol.[1]

About this Structure

3vzd is a 6 chain structure with sequence from Human. Full crystallographic information is available from OCA.

Reference

  1. Wang Z, Min X, Xiao SH, Johnstone S, Romanow W, Meininger D, Xu H, Liu J, Dai J, An S, Thibault S, Walker N. Molecular Basis of Sphingosine Kinase 1 Substrate Recognition and Catalysis. Structure. 2013 Apr 16. pii: S0969-2126(13)00086-5. doi:, 10.1016/j.str.2013.02.025. PMID:23602659 doi:https://dx.doi.org/10.1016/j.str.2013.02.025
  1. ↑ Alvarez SE, Harikumar KB, Hait NC, Allegood J, Strub GM, Kim EY, Maceyka M, Jiang H, Luo C, Kordula T, Milstien S, Spiegel S. Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2. Nature. 2010 Jun 24;465(7301):1084-8. doi: 10.1038/nature09128. PMID:20577214 doi:10.1038/nature09128

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