2osl
From Proteopedia
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Crystal structure of Rituximab Fab in complex with an epitope peptide
Overview
Rituximab is a widely used monoclonal antibody drug for treating certain, lymphomas and autoimmune diseases. To understand the molecular mechanism, of recognition of human CD20 by Rituximab, we determined the crystal, structure of the Rituximab Fab in complex with its cognate epitope peptide, from human CD20 (residues 163-187) at 2.6 A resolution. The combining site, of the Fab consists of four complementarity determining regions that form, a large, deep pocket to accommodate the epitope peptide. The bound peptide, assumes a unique cyclic conformation that is constrained by a disulfide, bond and a rigid proline residue (Pro172). The 170ANPS173 motif of CD20 is, deeply embedded into the pocket on the antibody surface and plays an, essential role in the recognition and binding of Rituximab. The, antigen-antibody interactions involve both hydrogen bonds and van der, Waals contacts and display a high degree of structural and chemical, complementarity. These results provide molecular basis for the specific, recognition of CD20 by Rituximab as well as valuable information for, development of improved antibody drugs with better specificity and higher, affinity.
About this Structure
2OSL is a Single protein structure of sequence from Homo sapiens, mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for recognition of CD20 by therapeutic antibody Rituximab., Du J, Wang H, Zhong C, Peng B, Zhang M, Li B, Huo S, Guo Y, Ding J, J Biol Chem. 2007 Mar 29;. PMID:17395584
Page seeded by OCA on Mon Nov 12 23:15:42 2007
