rituximab therapie 投稿者：Cleo 投稿日：2026/01/11(Sun) 06:29 No.3392106 
CD20 is a non-glycosylated phosphoprotein with 4 transmembrane domains and a big extracellular loop, which offers an accessible goal for antibody binding. Rituximab’s Fab area acknowledges a conformational epitope on this extracellular loop-key residues corresponding to these throughout the ANPS motif are critically concerned in binding. Binding results in the formation of a stable antigen-antibody advanced with out speedy internalization of the receptor, which is significant for sustained immune system engagement. This binding course of is extremely particular: utilizing methods equivalent to crystallography has revealed that upon binding, the cyclic peptide fragment derived from CD20 assumes a constrained conformation because of the presence of a disulfide bond and a inflexible proline residue. These structural options be certain that rituximab exhibits a excessive diploma of complementarity with the CD20 goal. Furthermore, by clustering CD20 molecules in lipid rafts, rituximab can improve signaling and successfully crosslink the B-cell receptors. The stability of the CD20-rituximab complicated is maintained throughout circulation, thereby permitting efficient opsonization and activation of downstream immune effector capabilities.
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