4LLQ: Structure of redesigned IgG1 first constant and lambda domains (CH1:Clambda constant redesign 2 beta, CRD2b) at 1.42A

Citation:
Abstract
Robust generation of IgG bispecific antibodies has been a long-standing challenge. Existing methods require extensive engineering of each individual antibody, discovery of common light chains, or complex and laborious biochemical processing. Here we combine computational and rational design approaches with experimental structural validation to generate antibody heavy and light chains with orthogonal Fab interfaces. Parental monoclonal antibodies incorporating these interfaces, when simultaneously co-expressed, assemble into bispecific IgG with improved heavy chain-light chain pairing. Bispecific IgGs generated with this approach exhibit pharmacokinetic and other desirable properties of native IgG, but bind target antigens monovalently. As such, these bispecific reagents may be useful in many biotechnological applications.
PDB ID: 4LLQDownload
MMDB ID: 117046
PDB Deposition Date: 2013/7/9
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.42  Å
Source Organism:
Similar Structures:
Biological Unit for 4LLQ: dimeric; determined by author and by software (PISA)
Molecular Components in 4LLQ
Label Count Molecule
Proteins (2 molecules)
1
Mutated CH1
Molecule annotation
1
Mutated Light Chain Clambda
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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