![]() We present crystal structures of EndoS2 alone and bound to complex and high-mannose glycans the broad N-glycan specificity is governed by critical loops that shape the binding site of EndoS2. EndoS2 is useful in these schemes because it accommodates a broad range of N-glycans, including high-mannose, complex, and hybrid types however, its mechanism of substrate recognition is poorly understood. ![]() EndoS2 and specific point mutants have been used to chemoenzymatically synthesize antibodies with customizable glycosylation for gain of functions. Streptococcus pyogenes secretes a unique endo-β- N-acetylglucosaminidase, EndoS2, which deglycosylates the conserved N-linked glycan at Asn297 on IgG Fc to eliminate its effector functions and evade the immune system. ![]() Immunoglobulin G (IgG) glycosylation critically modulates antibody effector functions. ![]()
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