Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

Werner Braun; Catherine H. Schein

doi:10.1016/j.str.2014.04.008

Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

Werner Braun, Catherine H. Schein

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

8 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
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Access to Document

10.1016/j.str.2014.04.008

Cite this

@article{93e0bbb2e74940b4ae40d67799dc0692,

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 Schein, {Catherine H.}",

year = "2014",

month = may,

day = "6",

doi = "10.1016/j.str.2014.04.008",

language = "English (US)",

volume = "22",

pages = "664--666",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "5",

}

TY - JOUR

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

AU - Braun, Werner

AU - Schein, Catherine H.

PY - 2014/5/6

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.

UR - http://www.scopus.com/inward/record.url?scp=84899821358&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84899821358&partnerID=8YFLogxK

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

EP - 666

JO - Structure

JF - Structure

IS - 5

ER -

Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this