Metadata |
datasetIdentifier | PASS00053 |
datasetType | XlinkMS |
submitter | Lars Malmstroem <lars@imsb.biol.ethz.ch> |
submitter_organization | |
lab_head_full_name | |
lab_head_email | |
lab_head_organization | |
lab_head_country | |
datasetTag | xlms_on_pp2a |
datasetTitle | Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-linking and Mass Spectrometry |
publicReleaseDate | 2012-07-26 00:00:00 |
finalizedDate | 2012-07-26 01:33:28 |
summary | Mass spectrometry is routinely applied to the identification and quantification of proteins and
post-translational modifications. By combining chemical cross-linking and mass spectrometry
(XL-MS), we gained structural information in the form of distance restraints on an interaction
network of protein complexes isolated from human cells. Systematic XL-MS analysis of
protein phosphatase 2A (PP2A) complexes identified 176 inter-protein and 569 intra-protein
spatial restraints that link specific trimeric PP2A complexes to a multitude of adaptor proteins
controlling its cellular function. Cross-links guided molecular modeling of the binding
interface between immunoglobulin-binding-protein-1 (IGBP1) and PP2A and revealed the
topology of a TCP-1-ring-complex (TRiC) chaperonin interacting with the PP2A regulatory
subunit Bγ. This study establishes XL-MS as an integral part of hybrid structural biology
approaches for the analysis of endogenous protein complexes.
|
contributors | Franz Herzog
Lars Malmstroem |
publication | Structural Probing of a Protein Phosphatase 2A Network by Chemical
Cross-linking and Mass Spectrometry
Franz Herzog Abdullah Kahraman Daniel Böhringer Raymond Mak Andreas
Bracher Thomas Walzthöni Alexander Leitner Martin Beck Franz-Ulrich Hartl Nenad
Ban Lars Malmström and Ruedi Aebersold
submitted |
growth | |
treatment | |
extraction | |
separation | |
digestion | |
acquisition | |
informatics | |
instruments | LTQ Orbitrap |
species | Human |
massModifications | static: C+57.021464
variable: K+156.0786442
variable: K+155.0964278 |