1OAX
Fv Structure of the IgE SPE-7 in complex with acenaphthenequinone
Summary for 1OAX
| Entry DOI | 10.2210/pdb1oax/pdb |
| Related | 1OAQ 1OAR 1OAU 1OAY 1OAZ |
| Descriptor | IMMUNOGLOBULIN E, ACENAPHTHENEQUINONE, ... (4 entities in total) |
| Functional Keywords | immune system, antibody-complex, antibody, allergy, ige |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Total number of polymer chains | 6 |
| Total formula weight | 73998.72 |
| Authors | James, L.C.,Roversi, P.,Tawfik, D. (deposition date: 2003-01-21, release date: 2004-01-15, Last modification date: 2024-11-20) |
| Primary citation | James, L.C.,Roversi, P.,Tawfik, D. Antibody Multispecificity Mediated by Conformational Diversity Science, 299:1362-, 2003 Cited by PubMed Abstract: A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre-steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy. PubMed: 12610298DOI: 10.1126/SCIENCE.1079731 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.67 Å) |
Structure validation
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