2osl

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(New page: 200px<br /> <applet load="2osl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2osl, resolution 2.600&Aring;" /> '''Crystal structure ...)
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caption="2osl, resolution 2.600&Aring;" />
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'''Crystal structure of Rituximab Fab in complex with an epitope peptide'''<br />
'''Crystal structure of Rituximab Fab in complex with an epitope peptide'''<br />
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==About this Structure==
==About this Structure==
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2OSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens,_mus_musculus Homo sapiens, mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OSL OCA].
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2OSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens,_mus_musculus Homo sapiens, mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OSL OCA].
==Reference==
==Reference==
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[[Category: rituximab]]
[[Category: rituximab]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:15:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:43:34 2008''

Revision as of 12:43, 23 January 2008


2osl, resolution 2.600Å

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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

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