1UZ6
anti-Lewis X Fab fragment uncomplexed
Summary for 1UZ6
| Entry DOI | 10.2210/pdb1uz6/pdb |
| Related | 1UZ8 |
| Descriptor | IGG FAB (IGG3, KAPPA) LIGHT CHAIN 291-2G3-A, IGG FAB (IGG3, KAPPA) HEAVY CHAIN 291-2G3-A, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | immune system, antibody-complex, antibody, anti-carbohydrate |
| Biological source | MUS MUSCULUS (MOUSE) More |
| Total number of polymer chains | 8 |
| Total formula weight | 190468.59 |
| Authors | Van Roon, A.M.M.,Pannu, N.S.,De Vrind, J.P.M.,Hokke, C.H.,Deelder, A.M.,Van Der marel, G.A.,Van Boom, J.H.,Abrahams, J.P. (deposition date: 2004-03-05, release date: 2004-06-29, Last modification date: 2024-11-13) |
| Primary citation | Van Roon, A.M.M.,Pannu, N.S.,De Vrind, J.P.M.,Van Der Marel, G.A.,Van Boom, J.H.,Hokke, C.H.,Deelder, A.M.,Abrahams, J.P. Structure of an Anti-Lewis X Fab Fragment in Complex with its Lewis X Antigen Structure, 12:1227-, 2004 Cited by PubMed Abstract: 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. PubMed: 15242599DOI: 10.1016/J.STR.2004.05.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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