3hc0

Publication Abstract from PubMed

Bispecific immunoglobulin-like antibodies capable of engaging multiple antigens represent a promising new class of therapeutic agents. Engineering of these molecules requires optimization of the molecular properties of one of the domain components. Here, we present a detailed crystallographic and computational characterization of the stabilization patterns in the lymphotoxin-beta receptor (LTbetaR) binding Fv domain of an anti-LTbetaR/anti-TNF-related apoptosis inducing ligand receptor-2 (TRAIL-R2) bispecific immunoglobulin-like antibody. We further describe a new hierarchical structure-guided approach toward engineering of antibody-like molecules to enhance their thermal and chemical stability. Proteins 2009. (c) 2009 Wiley-Liss, Inc.

Structural understanding of stabilization patterns in engineered bispecific Ig-like antibody molecules.,Jordan JL, Arndt JW, Hanf K, Li G, Hall J, Demarest S, Huang F, Wu X, Miller B, Glaser S, Fernandez EJ, Wang D, Lugovskoy A Proteins. 2009 Jun 19. PMID:19626705^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.