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Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry

The identification of proximate amino acids by chemical cross-linking and mass spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes. We gained distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying...

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Bibliographic Details
Main Authors: Herzog, Franz (Author) , Böhringer, Daniel (Author) , Beck, Martin (Author)
Format: Article (Journal)
Language:English
Published: 14 September 2012
In: Science
Year: 2012, Volume: 337, Issue: 6100, Pages: 1348-1352
ISSN:1095-9203
DOI:10.1126/science.1221483
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1126/science.1221483
Verlag, kostenfrei, Volltext: http://science.sciencemag.org/content/337/6100/1348
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Author Notes:Franz Herzog, Abdullah Kahraman, Daniel Boehringer, Raymond Mak, Andreas Bracher, Thomas Walzthoeni, Alexander Leitner, Martin Beck, Franz-Ulrich Hartl, Nenad Ban, Lars Malmström, Ruedi Aebersold
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Summary:The identification of proximate amino acids by chemical cross-linking and mass spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes. We gained distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying an adapted XL-MS protocol. Systematic analysis of human protein phosphatase 2A (PP2A) complexes identified 176 interprotein and 570 intraprotein cross-links that link specific trimeric PP2A complexes to a multitude of adaptor proteins that control their cellular functions. Spatial restraints guided molecular modeling of the binding interface between immunoglobulin binding protein 1 (IGBP1) and PP2A and revealed the topology of TCP1 ring complex (TRiC) chaperonin interacting with the PP2A regulatory subunit 2ABG. This study establishes XL-MS as an integral part of hybrid structural biology approaches for the analysis of endogenous protein complexes. Spatial restraints revealed by chemical cross-linking and mass spectrometry elucidate the topology of a dynamic signaling network.
Item Description:Gesehen am 08.10.2018
Physical Description:Online Resource
ISSN:1095-9203
DOI:10.1126/science.1221483

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