Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

Werner Braun; Catherine Braun-Schein

doi:10.1016/j.str.2014.04.008

Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

Werner Braun
, Catherine Braun-Schein

Biochemistry & Molecular Biology

Research output: Contribution to journal › Short survey › peer-review

9 Scopus citations

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.

Original language	English (US)
Pages (from-to)	664-666
Number of pages	3
Journal	Structure
Volume	22
Issue number	5
DOIs	https://doi.org/10.1016/j.str.2014.04.008
State	Published - May 6 2014

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.str.2014.04.008

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title = "Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases",

abstract = "In this issue of Structure, Tr{\'e}saugues 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.",

author = "Werner Braun and Catherine Braun-Schein",

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T1 - Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

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AU - Braun-Schein, Catherine

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Y1 - 2014/5/6

N2 - 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.

AB - 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.

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UR - https://www.scopus.com/pages/publications/84899821358#tab=citedBy

U2 - 10.1016/j.str.2014.04.008

DO - 10.1016/j.str.2014.04.008

M3 - Short survey

C2 - 24807076

AN - SCOPUS:84899821358

SN - 0969-2126

VL - 22

SP - 664

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JO - Structure

JF - Structure

IS - 5

ER -

Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

Abstract

ASJC Scopus subject areas

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