4IML
CrossFab binding to human Angiopoietin 2
Summary for 4IML
| Entry DOI | 10.2210/pdb4iml/pdb |
| Related | 4IMK |
| Descriptor | Crossed heavy chain (VH-Ckappa), Crossed light chain (VL-CH1), GLYCEROL, ... (4 entities in total) |
| Functional Keywords | crossfab, antigen binding, human angiopoietin 2, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 4 |
| Total formula weight | 98779.18 |
| Authors | Fenn, S.,Schiller, C.,Griese, J.,Hopfner, K.-P.,Kettenberger, H. (deposition date: 2013-01-03, release date: 2013-04-17, Last modification date: 2024-11-20) |
| Primary citation | Fenn, S.,Schiller, C.B.,Griese, J.J.,Duerr, H.,Imhof-Jung, S.,Gassner, C.,Moelleken, J.,Regula, J.T.,Schaefer, W.,Thomas, M.,Klein, C.,Hopfner, K.P.,Kettenberger, H. Crystal Structure of an Anti-Ang2 CrossFab Demonstrates Complete Structural and Functional Integrity of the Variable Domain. Plos One, 8:e61953-e61953, 2013 Cited by PubMed 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. PubMed: 23613981DOI: 10.1371/journal.pone.0061953 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.931 Å) |
Structure validation
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