Proteomics

Dataset Information

0

Quantitative cross-linking/mass spectrometry analysis revealed unknown structure of complement iC3

ABSTRACT: We applied quantitative cross-linking/mass spectrometry (QCLMS) to interrogate the structure of iC3 (or C3(H2O)), the activated hydrolytic product of the abundant human complement protein C3. The slow but spontaneous and ubiquitous formation of iC3 from C3 initiates antibody-independent activation of the complement system that is a key first line of antimicrobial defense. QCLMS revealed structural differences and similarities between iC3 and C3, as well as between iC3 and C3b that is a pivotal proteolytic cleavage product of C3 and is functionally similar to iC3. Considered in combination with the crystal structures of C3 and C3b, our data support a model wherein the thioester-containing domain of C3 swings to the other end of the molecule creating, in iC3, a stable C3b-like platform for binding the zymogen, factor B, or the regulator, factor H. The integration of available crystallographic and QCLMS data allowed the determination of a 3D model for iC3. The unique arrangement of domains in iC3, which retains the anaphylatoxin (ANA) domain (while ANA is excised when C3 is enzymatically activated to C3b), is consistent with observed differences in activation and regulation between iC3 and C3b.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Zhuo Chen  

LAB HEAD: Juri Rappsilber

PROVIDER: PXD003486 | Pride | 2016-06-17

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
Chen_Rappsilber_QCLMS_xC3bd0iC3d4_I.raw Raw
Chen_Rappsilber_QCLMS_xC3bd0iC3d4_II.raw Raw
Chen_Rappsilber_QCLMS_xC3bd4iC3d0_I.raw Raw
Chen_Rappsilber_QCLMS_xC3bd4iC3d0_II.raw Raw
Chen_Rappsilber_QCLMS_xC3d0iC3d4_I.raw Raw
Items per page:
1 - 5 of 10
altmetric image

Publications

Structure of Complement C3(H2O) Revealed By Quantitative Cross-Linking/Mass Spectrometry And Modeling.

Chen Zhuo A ZA   Pellarin Riccardo R   Fischer Lutz L   Sali Andrej A   Nilges Michael M   Barlow Paul N PN   Rappsilber Juri J  

Molecular & cellular proteomics : MCP 20160601 8

The slow but spontaneous and ubiquitous formation of C3(H2O), the hydrolytic and conformationally rearranged product of C3, initiates antibody-independent activation of the complement system that is a key first line of antimicrobial defense. The structure of C3(H2O) has not been determined. Here we subjected C3(H2O) to quantitative cross-linking/mass spectrometry (QCLMS). This revealed details of the structural differences and similarities between C3(H2O) and C3, as well as between C3(H2O) and i  ...[more]

Similar Datasets

Proteomics Quantitative cross-linking/mass spectrometry reveals subtle protein conformational changes
2016-06-16 | PXD001675 | Pride
Proteomics A model dataset for quantitative cross-linking/mass spectrometry using isotope-labeled cross-linkers
2016-05-06 | PXD004107 | Pride
Proteomics Data independent acquisition cross-linking/mass spectrometry
2019-01-25 | PXD011036 | Pride
Proteomics Quantitative cross-linking/mass spectrometry
2015-06-08 | PXD002142 | Pride
Proteomics On the reproducibility of label-free quantitative cross-linking/mass spectrometry
2018-01-02 | PXD007250 | Pride
Proteomics Cross-linking mass spectrometry of yeast mitochondria grown on different carbon sources reveal Ndi1, Min8 and Pet9 associated with the electron transport chain
2020-04-27 | PXD017620 | Pride
Proteomics An integrated workflow for cross-linking/mass spectrometry
2019-08-27 | PXD008550 | Pride
Proteomics Aurora B kinase disrupts the extended conformation of lattice-bound Kinesin-13 MCAK
2019-01-07 | PXD008215 | Pride
Proteomics Modeling flexible protein structure with AlphaFold2 and cross-linking mass spectrometry
2024-05-24 | PXD046392 | Pride
Proteomics Capturing protein communities by structural proteomics in a thermophilic eukaryote
2017-07-26 | PXD006626 | Pride