PXD076459-1

PXD076459 is an original dataset announced via ProteomeXchange.

Title	Multiple disulfide-bonded states confer conformational diversity in fibrinogen
Description	Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms. This hypothesis was tested by resolving fibrinogen molecules on beads coated with different fibrinogen ligands and measuring their disulfide states by differential cysteine alkylation and mass spectrometry. Polyclonal anti-fibrinogen antibodies resolved states where all 11 measured disulfides across the molecule were significantly less formed. In contrast, the GHRP peptide, which binds the fibrinogen β-nodule, resolved states in which seven β-nodule and central E region disulfides were significantly more formed, while the GPRP peptide, which binds the γ-nodule, resolved states in which only one disulfide was significantly more formed. To probe the link between disulfide state and conformation, in silico analysis of all 32 possible disulfide-bonded states of the β-nodule revealed that the conformational flexibility of this domain and predicted GHRP interactions in its binding pocket are predicated on the oxidation state of one of the five β-nodule disulfides, βC424-βC437. These findings indicate that the different disulfide-bonded states of fibrinogen adopt an extensive array of conformations that are selectively recognized by different fibrinogen ligands.
HostingRepository	PRIDE
AnnounceDate	2026-04-13
AnnouncementXML	Submission_2026-04-12_16:11:05.733.xml
DigitalObjectIdentifier	https://doi.org/10.6019/PXD076459
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Aster Pijning
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2026-04-01 06:12:34	ID requested
⏵ 1	2026-04-12 16:11:06	announced

Pijning AE, Butera D, Hogg PJ, Multiple disulfide-bonded states confer extensive conformational diversity in fibrinogen. Protein Sci, 35(5):e70558(2026) [pubmed]

10.1002/pro.70558;

10.6019/PXD076459;

submitter keyword: Human, fibrinogen, disulfide bonds

Philip J. Hogg
contact affiliation	School of Life Sciences, University of Technology Sydney, Faculty of Science, Sydney, New South Wales, Australia Centenary Institute, University of Sydney, Sydney, New South Wales, Australia
contact email	phil.hogg@sydney.edu.au
lab head
Aster Pijning
contact affiliation	Centenary Insitute, The University of Sydney
contact email	a.pijning@centenary.org.au
dataset submitter

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/2026/04/PXD076459

PRIDE project URI

• PRIDE
  1. PXD076459
     1. Label: PRIDE project
     2. Name: Multiple disulfide-bonded states confer conformational diversity in fibrinogen