Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases
- PMID: 24807076
- DOI: 10.1016/j.str.2014.04.008
Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases
Abstract
In this issue of Structure, Trésaugues and colleagues determined the interaction of membrane-bound phosphoinositides with three clinically significant human inositol polyphosphate 5-phosphatases (I5Ps). A comparison to the structures determined with soluble substrates revealed differences in the binding mode and suggested how the I5Ps and apurinic endonuclease (APE1) activities evolved from the same metal-binding active center.
Copyright © 2014 Elsevier Ltd. All rights reserved.
Comment on
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Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases.Structure. 2014 May 6;22(5):744-55. doi: 10.1016/j.str.2014.01.013. Epub 2014 Apr 3. Structure. 2014. PMID: 24704254
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