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  Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry

Herzog, F., Kahraman, A., Boehringer, D., Mak, R., Bracher, A., Walzthoeni, T., et al. (2012). Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry. SCIENCE, 337(6100), 1348-1352. doi:10.1126/science.1221483.

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 Creators:
Herzog, Franz1, Author
Kahraman, Abdullah1, Author
Boehringer, Daniel2, Author              
Mak, Raymond1, Author
Bracher, Andreas3, Author              
Walzthoeni, Thomas1, Author
Leitner, Alexander1, Author
Beck, Martin1, Author              
Hartl, Franz-Ulrich3, Author              
Ban, Nenad1, Author
Malmstroem, Lars1, Author
Aebersold, Ruedi1, Author
Affiliations:
1external, ou_persistent22              
2Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              
3Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: MOLECULAR ARCHITECTURE; CRYSTAL-STRUCTURE; CHAPERONIN; COMPLEX; IDENTIFICATION; OPTIMIZATION; CONFORMATION; TRIC/CCT; ALPHA-4; BINDING
 Abstract: 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.

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Language(s): eng - English
 Dates: 2012-09-14
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000308705000044
DOI: 10.1126/science.1221483
 Degree: -

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Title: SCIENCE
Source Genre: Journal
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Publ. Info: 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA : AMER ASSOC ADVANCEMENT SCIENCE
Pages: - Volume / Issue: 337 (6100) Sequence Number: - Start / End Page: 1348 - 1352 Identifier: ISSN: 0036-8075