Structure of a human IgA1 Fab fragment at 1.55 Å resolution: potential effect of the constant domains on antigen-affinity modulation

Correa, A.; Trajtenberg, F.; Obal, G.; Pritsch, O.; Dighiero, G.; Oppezzo, P.; Buschiazzo, A.

doi:10.1107/S0907444912048664

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 1
Proteolytic generation of FabA fragments with different glycosylation patterns. (a) Schematic representation of the human IgA1 hinge region. The O-glycosylation sites (CHO) and IgA-protease cleavage sites are indicated. Note the complete avoidance of final glycosylation when using the C. ramosum protease. (b) SDS–PAGE showing the purified FabA fragments after C. ramosum (FabAr) or N. gonorrhoeae (FabAg) proteolytic cleavage. LC, light chain; Fd, heavy-chain portion of the Fab fragment.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 69| Part 3| February 2013| Pages 388-397

doi:10.1107/S0907444912048664

Follow Acta Cryst. D

Search IUCr Journals		doi		Advanced search
Author		volume	page