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PDBsum entry 4imk

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Top Page protein ligands metals Protein-protein interface(s) links
Immune system PDB id
4imk
Contents
Protein chains
229 a.a.
213 a.a.
Ligands
GOL ×2
SO4
Metals
_NA
Waters ×319

References listed in PDB file
Key reference
Title Crystal structure of an anti-Ang2 crossfab demonstrates complete structural and functional integrity of the variable domain.
Authors S.Fenn, C.B.Schiller, J.J.Griese, H.Duerr, S.Imhof-Jung, C.Gassner, J.Moelleken, J.T.Regula, W.Schaefer, M.Thomas, C.Klein, K.P.Hopfner, H.Kettenberger.
Ref. Plos One, 2013, 8, e61953. [DOI no: 10.1371/journal.pone.0061953]
PubMed id 23613981
Abstract
Bispecific antibodies are considered as a promising class of future biotherapeutic molecules. They comprise binding specificities for two different antigens, which may provide additive or synergistic modes of action. There is a wide variety of design alternatives for such bispecific antibodies, including the "CrossMab" format. CrossMabs contain a domain crossover in one of the antigen-binding (Fab) parts, together with the "knobs-and-holes" approach, to enforce the correct assembly of four different polypeptide chains into an IgG-like bispecific antibody. We determined the crystal structure of a hAng-2-binding Fab in its crossed and uncrossed form and show that CH1-CL-domain crossover does not induce significant perturbations of the structure and has no detectable influence on target binding.
PROCHECK
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