Antibody fucosylation lowers FcγRIIIa/CD16a affinity by limiting the conformations sampled by the N162-glycan

समान संसाधन

• Restricted motion of the conserved immunoglobulin G1 N-glycan is essential for efficient FcγRIIIa binding
  द्वारा: Subedi, Ganesh P., और अन्य
  प्रकाशित: (2014)
• CD16a with oligomannose-type N-glycans is the only “low-affinity” Fc γ receptor that binds the IgG crystallizable fragment with high affinity in vitro
  द्वारा: Subedi, Ganesh P., और अन्य
  प्रकाशित: (2018)
• The immunoglobulin G1 N-glycan composition affects binding to each low affinity Fc γ receptor
  द्वारा: Subedi, Ganesh P., और अन्य
  प्रकाशित: (2016)
• The N-linked oligosaccharide at FcγRIIIa Asn-45: an inhibitory element for high FcγRIIIa binding affinity to IgG glycoforms lacking core fucosylation
  द्वारा: Shibata-Koyama, Mami, और अन्य
  प्रकाशित: (2009)
• Restricted processing of CD16a/Fc γ receptor IIIa N-glycans from primary human NK cells impacts structure and function
  द्वारा: Patel, Kashyap R., और अन्य
  प्रकाशित: (2018)