1AD0

FAB FRAGMENT OF ENGINEERED HUMAN MONOCLONAL ANTIBODY A5B7

Summary for 1AD0

• Entry DOI: 10.2210/pdb1ad0/pdb
• Descriptor: ANTIBODY A5B7 (LIGHT CHAIN), ANTIBODY A5B7 (HEAVY CHAIN) (3 entities in total)
• Functional Keywords: immunoglobulin, fab fragment
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 94026.71

Authors

Banfield, M.J.,Brady, R.L. (deposition date: 1997-02-19, release date: 1998-02-25, Last modification date: 2024-11-20)

Primary citation

Banfield, M.J.,King, D.J.,Mountain, A.,Brady, R.L.
VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs.
Proteins, 29:161-171, 1997

PubMed Abstract: The crystal structures of two pairs of Fab fragments have been determined. The pairs comprise both a murine and an engineered human form, each derived from the antitumor antibodies A5B7 and CTM01. Although antigen specificity is maintained within the pairs, antigen affinity varies. A comparison of the hypervariable loops for each pair of antibodies shows their structure has been well maintained in grafting, supporting the canonical loop model. Detailed structural analysis of the binding sites and domain arrangements for these antibodies suggests the differences in antigen affinity observed are likely to be due to inherent flexibility of the hypervariable loops and movements at the VL:VH domain interface. The four structures provide the first opportunity to study in detail the effects of protein engineering on specific antibodies.

PubMed: 9329081
DOI: 10.1002/(SICI)1097-0134(199710)29:2<161::AID-PROT4>3.0.CO;2-G

Experimental method

X-RAY DIFFRACTION (2.5 Å)