1uz6: Difference between revisions
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==Overview== | ==Overview== | ||
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 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. | ||
==About this Structure== | ==About this Structure== | ||
1UZ6 is a | 1UZ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UZ6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: antibody]] | [[Category: antibody]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:10:34 2007'' | ||
Revision as of 14:05, 5 November 2007
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ANTI-LEWIS X FAB FRAGMENT UNCOMPLEXED
OverviewOverview
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.
About this StructureAbout this Structure
1UZ6 is a Single protein structure of sequence from Mus musculus with SO4 as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Structure of an anti-Lewis X Fab fragment in complex with its Lewis X antigen., van Roon AM, Pannu NS, de Vrind JP, van der Marel GA, van Boom JH, Hokke CH, Deelder AM, Abrahams JP, Structure. 2004 Jul;12(7):1227-36. PMID:15242599
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