X836 light chain. Chain: l. Engineered: yes. X836 heavy chain. Chain: h. Fragment: chimeric molecule of mouse variable domain and human constant domain, fd fragment. Engineered: yes
Source:
Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell: human embryonic kidney (hek) 293 cells. Mus musculus, homo sapiens. Mouse, human. Organism_taxid: 10090,9606.
Resolution:
1.60Å
R-factor:
0.211
R-free:
0.232
Authors:
A.Teplyakov,G.Obmolova,G.L.Gilliland
Key ref:
A.Teplyakov
et al.
(2010).
On the domain pairing in chimeric antibodies.
Mol Immunol,
47,
2422-2426.
PubMed id: 20554002
A chimeric antibody was constructed from two unrelated antibodies by combining
their heavy and light chains. The "double chimera" consists of the mouse
variable regions of different specificity (IL-13 and EMMPRIN) and the constant
regions of different origin (mouse and human). The Fab fragment of this chimeric
antibody was expressed in mammalian cells, and the crystal structure was
determined at 1.6A resolution. Despite a large number of amino acid
substitutions in the double chimera with respect to the parent antibodies, the
heavy and light chains associate into a stable molecule. Comparison to the
structure of one of the parent antibodies reveals that the variable domain
interface, as well as the conformation of antigen-binding loops, is preserved
without major rearrangements due to conservation of amino acids in key
positions. Comparison to the structures of the all-human and all-mouse constant
domains indicates a remarkable plasticity of the inter-chain interface that can
tolerate residue relocations of up to 6A.
Links
