PXD003486 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Quantitative cross-linking/mass spectrometry analysis revealed unknown structure of complement iC3 |
Description | 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. |
HostingRepository | PRIDE |
AnnounceDate | 2016-06-17 |
AnnouncementXML | Submission_2016-06-17_02:30:31.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Zhuo Chen |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2016-01-19 01:57:17 | ID requested | |
⏵ 1 | 2016-06-17 02:30:32 | announced | |
Publication List
Chen ZA, Pellarin R, Fischer L, Sali A, Nilges M, Barlow PN, Rappsilber J, Structure of Complement C3(H2O) Revealed By Quantitative Cross-Linking/Mass Spectrometry And Modeling. Mol Cell Proteomics, 15(8):2730-43(2016) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Quantitative cross-linking/mass spectrometry |
domain architecture |
activation of complement system |
alternative pathway |
Contact List
Juri Rappsilber |
contact affiliation | 1. Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, UK 2. Department of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Germany |
contact email | juri.rappsilber@ed.ac.uk |
lab head | |
Zhuo Chen |
contact affiliation | University of Edinburgh |
contact email | zhuo.chen@ed.ac.uk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2016/06/PXD003486 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD003486
- Label: PRIDE project
- Name: Quantitative cross-linking/mass spectrometry analysis revealed unknown structure of complement iC3