Stacking and energetic contribution of aromatic islands at the binding interface of antibody proteins.

ABSTRACT:

Background

The enrichment and importance of some aromatic residues, such as Tyr and Trp, have been widely noticed at the binding interfaces of antibodies from many experimental and statistical results, some of which were even identified as "hot spots" contributing significantly greater to the binding affinity than other amino acids. However, how these aromatic residues influence the immune binding still deserves further investigation. A large-scale examination was done regarding the local spatial environment around the interfacial Tyr or Trp residues. Energetic contribution of these Tyr and Trp residues to the binding affinity was then studied regarding 82 representative antibody interfaces covering 509 immune complexes from the PDB database and IMGT/3Dstructure-DB.

Results

SUBMITTER: Wu D 

PROVIDER: S-EPMC2946779 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature