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1OAU

Fv Structure of the IgE SPE-7 in complex with DNP-Ser (immunising hapten)

Summary for 1OAU
Entry DOI10.2210/pdb1oau/pdb
Related1OAQ 1OAR 1OAX 1OAY 1OAZ
DescriptorIMMUNOGLOBULIN E, SERINE, 2,4-DINITROPHENOL, ... (6 entities in total)
Functional Keywordsimmune system, antibody-complex, antibody, allergy, ige, conformational diversity, multispecificity
Biological sourceMUS MUSCULUS (HOUSE MOUSE)
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Total number of polymer chains8
Total formula weight101589.06
Authors
James, L.C.,Roversi, P.,Tawfik, D. (deposition date: 2003-01-21, release date: 2004-01-15, Last modification date: 2024-10-23)
Primary citationJames, 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: 12610298
DOI: 10.1126/SCIENCE.1079731
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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