4IMK

Uncrossed Fab binding to human Angiopoietin 2

Summary for 4IMK

• Entry DOI: 10.2210/pdb4imk/pdb
• Related: 4IML
• Descriptor: Heavy Chain, Light Chain, SODIUM ION, ... (6 entities in total)
• Functional Keywords: antigen-binding fragment (fab), human angiopoietin 2, immune system
• Biological source: Homo sapiens; More
• Total number of polymer chains: 4
• Total formula weight: 98369.76

Authors

Fenn, S.,Schiller, C.,Griese, J.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

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: 23613981
DOI: 10.1371/journal.pone.0061953

Experimental method

X-RAY DIFFRACTION (2.202 Å)