PDB FilesRedundancyStructural VariabilityAccessibilityAntigen ContactsDimer ContactsTorsion AnglesHydrogen Bonds

VL/VH Dimer Interface

Given the combinatorial nature of antibody generation, the dimer interface residues have to be such that any VL domain can pair with any VH domain to form a functional interface. This places a heavy constraint on the conservation of the interface residues.
VL Dimer Contacts
VH Dimer Contacts
At the same time, there is considerable overlap between the antigen interface and the dimer interface, particularely for hapten-binding antibodies, where the antigen frequently inserts into a deep binding pocket in the center of the barrel formed by the inner beta sheets of the two domains.
This can be clearly seen in a comparison of antigen interactions and VL/VH dimer interactions in anti-Hapten, anti-Oligomer and anti-Protein antibodies or from a comparison of the dimer and antigen contact histograms (see below)

Dimer contact residues in individual domains are listed in the following pages:

AAAAA Homepage Zürich University Dept. of Biochemistry Plückthun Group Annemarie Honegger

Last Modified by A.Honegger Wednesday, January 26, 2005