1OAY: Antibody Multispecificity Mediated By Conformational Diversity

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.
PDB ID: 1OAYDownload
MMDB ID: 98453
PDB Deposition Date: 2003/1/21
Updated in MMDB: 2013/10
Experimental Method:
x-ray diffraction
Resolution: 2.66  Å
Source Organism:
Similar Structures:
Biological Unit for 1OAY: dimeric; determined by author and by software (PQS)
Molecular Components in 1OAY
Label Count Molecule
Proteins (2 molecules)
Immunoglobulin E
Molecule annotation
Immunoglobulin E
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB