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3HC4

BHA10 IgG1 Fab quadruple mutant variant - antibody directed at human LTBR

Summary for 3HC4
Entry DOI10.2210/pdb3hc4/pdb
Related3HC0
DescriptorIMMUNOGLOBULIN IGG1 FAB, HEAVY CHAIN, IMMUNOGLOBULIN IGG1 FAB, LIGHT CHAIN, ACETATE ION, ... (5 entities in total)
Functional Keywordsigg1 fab, bha10, immune system
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight46566.41
Authors
Arndt, J.W.,Jordan, J.L.,Lugovskoy, A.,Wang, D. (deposition date: 2009-05-05, release date: 2009-08-04, Last modification date: 2023-09-06)
Primary citationJordan, 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: 19626705
DOI: 10.1002/prot.22502
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.62 Å)
Structure validation

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