Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases

Werner Braun, Catherine H. Schein

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)664-666
Number of pages3
JournalStructure
Volume22
Issue number5
DOIs
StatePublished - May 6 2014

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DNA-(Apurinic or Apyrimidinic Site) Lyase
Membranes
Phosphatidylinositols
Metals
Inositol Polyphosphate 5-Phosphatases

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Membrane interaction and functional plasticity of inositol polyphosphate 5-phosphatases. / Braun, Werner; Schein, Catherine H.

In: Structure, Vol. 22, No. 5, 06.05.2014, p. 664-666.

Research output: Contribution to journalArticle

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