1UZ8: Anti-Lewis X Fab Fragment In Complex With Lewis X
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
ID 4531043
Author(s) Van Roon, AMM; Pannu, NS; De Vrind, JPM; Hokke, CH; Deelder, AM; Van Der Marel, GA; Van Boom, JH; Abrahams, JP
Author(s) at UniBasel Abrahams, Jan Pieter
Year 2004
Title 1UZ8: Anti-Lewis X Fab Fragment In Complex With Lewis X
Journal Worldwide Protein Data Bank
Pages / Article-Number 1UZ8
Keywords Immune system
Mesh terms Science & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyBiochemistry & Molecular Biology

The Lewis X trisaccharide is pivotal in mediating specific cell-cell interactions. Monoclonal antibody 291-2G3-A, which was generated from mice infected with schistosomes, has been shown to recognize the Lewis X trisaccharide. Here we describe the structure of the Fab fragment of 291-2G3-A, with Lewis X, to 1.8 A resolution. The crystallographic analysis revealed that the antigen binding site is a rather shallow binding pocket, and residues from all six complementary determining regions of the antibody contact all sugar residues. The high specificity of the binding pocket does not result in high affinity; the K(D) determined by isothermal calorimetry is 11 microM. However, this affinity is in the same range as for other sugar-antibody complexes. The detailed understanding of the antibody-Lewis X interaction revealed by the crystal structure may be helpful in the design of better diagnostic tools for schistosomiasis and for studying Lewis X-mediated cell-cell interactions by antibody interference.

Full Text on edoc
Digital Object Identifier DOI 10.2210/pdb1uz8/pdb
ISI-Number DRCI:DATA2012137001735311
Document type (ISI) Data set

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