6 research outputs found
Mechanism of Dimerization of a Recombinant Mature Vascular Endothelial Growth Factor C
The
vascular endothelial growth factors (VEGFs) and their tyrosine
kinase receptors play a pivotal role in angiogenesis and lymphangiogenesis
during development and in pathologies such as tumor growth. The VEGFs
function as disulfide-linked antiparallel homodimers. The lymphangiogenic
factors, VEGF-C and VEGF-D, exist as monomers and dimers, and dimerization
is regulated by a unique unpaired cysteine. In this study, we have
characterized the redox state of this unpaired cysteine in a recombinant
mature monomeric and dimeric VEGF-C by mass spectrometry. Our findings
indicate that the unpaired cysteine regulates dimerization via thiol–disulfide
exchange involving the interdimer disulfide bond
Table S2
Excel spreadsheet of labile disulphide bonds present in some molecules of a protein crystal but absent in others (same PDB, sheet 1), or present in some structures of a protein but absent in others (different PDB, sheet 2)
Table S1
Excel spreadsheet of unique disulphides in a culled set of X-ray structures described by G. Wang and R. Dunbrack, Jr. (file pdbaanr)
Supplementary material from Identification of allosteric disulfides from labile bonds in X-ray structures
Table S3, Figures S1-S
Table S2 from Identification of allosteric disulfides from labile bonds in X-ray structures
Excel spreadsheet of labile disulphide bonds present in some molecules of a protein crystal but absent in others (same PDB, sheet 1), or present in some structures of a protein but absent in others (different PDB, sheet 2)
Table S1 from Identification of allosteric disulfides from labile bonds in X-ray structures
Excel spreadsheet of unique disulphides in a culled set of X-ray structures described by G. Wang and R. Dunbrack, Jr. (file pdbaanr)