3HC3
BHA10 IgG1 Fab double mutant variant - antibody directed at human LTBR
Summary for 3HC3
Entry DOI | 10.2210/pdb3hc3/pdb |
Related | 3HC0 3HC4 |
Descriptor | IMMUNOGLOBULIN IGG1 FAB, LIGHT CHAIN, IMMUNOGLOBULIN IGG1 FAB, HEAVY CHAIN, ACETATE ION, ... (5 entities in total) |
Functional Keywords | igg1 fab, bha10, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 46994.96 |
Authors | Arndt, J.W.,Jordan, J.L.,Lugovskoy, A.,Wang, D. (deposition date: 2009-05-05, release date: 2009-08-04, Last modification date: 2024-10-16) |
Primary citation | Jordan, J.L.,Arndt, J.W.,Hanf, K.,Li, G.,Hall, J.,Demarest, S.,Huang, F.,Wu, X.,Miller, B.,Glaser, S.,Fernandez, E.J.,Wang, D.,Lugovskoy, A. Structural understanding of stabilization patterns in engineered bispecific Ig-like antibody molecules Proteins, 77:832-841, 2009 Cited by PubMed Abstract: 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. PubMed: 19626705DOI: 10.1002/prot.22502 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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