The Structure of the SPOP-Pdx1 Interface Reveals Insights into the Phosphorylation-Dependent Binding Regulation

Michael Sebastian Ostertag; Ana Cristina Messias; Michael Sattler; Grzegorz Maria Popowicz

doi:10.1016/j.str.2018.10.005

The Structure of the SPOP-Pdx1 Interface Reveals Insights into the Phosphorylation-Dependent Binding Regulation

Michael Sebastian Ostertag
, Ana Cristina Messias
, Michael Sattler
, Grzegorz Maria Popowicz

Chair of Biomolecular NMR-Spectroscopy

Helmholtz Zentrum München German Research Center for Environmental Health
Technical University of Munich

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Ostertag et al. solved the co-crystal structure of SPOP and Pdx1 and studied the effects of Pdx1 phosphorylation on SPOP binding strength. The interaction of the proteins leads to Pdx1 degradation and is considered a key regulatory mechanism for insulin homeostasis.

Original language	English
Pages (from-to)	327-334.e3
Journal	Structure
Volume	27
Issue number	2
DOIs	https://doi.org/10.1016/j.str.2018.10.005
State	Published - 5 Feb 2019

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

NMR
Pdx1
SPOP
affinity
beta-cells
crystallography
diabetes
protein
structure determination

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10.1016/j.str.2018.10.005

Cite this

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title = "The Structure of the SPOP-Pdx1 Interface Reveals Insights into the Phosphorylation-Dependent Binding Regulation",

abstract = "Ostertag et al. solved the co-crystal structure of SPOP and Pdx1 and studied the effects of Pdx1 phosphorylation on SPOP binding strength. The interaction of the proteins leads to Pdx1 degradation and is considered a key regulatory mechanism for insulin homeostasis.",

keywords = "NMR, Pdx1, SPOP, affinity, beta-cells, crystallography, diabetes, protein, structure determination",

author = "Ostertag, \{Michael Sebastian\} and Messias, \{Ana Cristina\} and Michael Sattler and Popowicz, \{Grzegorz Maria\}",

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AU - Ostertag, Michael Sebastian

AU - Messias, Ana Cristina

AU - Sattler, Michael

AU - Popowicz, Grzegorz Maria

PY - 2019/2/5

Y1 - 2019/2/5

N2 - Ostertag et al. solved the co-crystal structure of SPOP and Pdx1 and studied the effects of Pdx1 phosphorylation on SPOP binding strength. The interaction of the proteins leads to Pdx1 degradation and is considered a key regulatory mechanism for insulin homeostasis.

AB - Ostertag et al. solved the co-crystal structure of SPOP and Pdx1 and studied the effects of Pdx1 phosphorylation on SPOP binding strength. The interaction of the proteins leads to Pdx1 degradation and is considered a key regulatory mechanism for insulin homeostasis.

KW - NMR

KW - Pdx1

KW - SPOP

KW - affinity

KW - beta-cells

KW - crystallography

KW - diabetes

KW - protein

KW - structure determination

UR - https://www.scopus.com/pages/publications/85060718527

U2 - 10.1016/j.str.2018.10.005

DO - 10.1016/j.str.2018.10.005

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AN - SCOPUS:85060718527

SN - 0969-2126

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JO - Structure

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ER -

The Structure of the SPOP-Pdx1 Interface Reveals Insights into the Phosphorylation-Dependent Binding Regulation

Abstract

UN SDGs

Keywords

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