A chemical approach to immunoprotein engineering: chemoselective functionalization of thioester proteins in their native state.
Less than 6 feet under: Serum proteins C3, C4, and alpha(2)M each contain a thioester domain buried within a hydrophobic pocket, which is thought to shield the labile thioester from hydrolysis. Herein, we make use of the inherent reactivity of the hydrazide for thioester moieties to chemoselectively label these crucial serum regulators in their native conformation; this demonstrates that access to the thioester site is much greater than previously supposed.
Cole
Michael A
MA
The Scripps-Oxford Laboratory, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Tully
Sarah E
SE
Dodds
Alister W
AW
Arnold
James N
JN
Boldt
Grant E
GE
Sim
Robert B
RB
Offer
John
J
Wentworth
Paul
P
D001710:Biotin / Q000737:chemistry; D003176:Complement C3 / Q000737:chemistry* / Q000276:immunology; D015935:Complement C4b / Q000737:chemistry* / Q000276:immunology; D005456:Fluorescent Dyes / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D015202:Protein Engineering; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D000511:alpha-Macroglobulins / Q000737:chemistry* / Q000276:immunology
D003176:Complement C3; D005456:Fluorescent Dyes; D010455:Peptides; D013438:Sulfhydryl Compounds; D000511:alpha-Macroglobulins; D001710:Biotin; D015935:Complement C4b