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- Title
- Structural mechanism of the antigen recognition by the L1 cell adhesion molecule antibody A10-A3
- Author(s)
- C H Wei; E S Lee; J Y Jeon; Y S Heo; Seung Jun Kim; Y H Jeon; K H Kim; H J Hong; S E Ryu
- Bibliographic Citation
- FEBS Letters, vol. 585, no. 1, pp. 153-158
- Publication Year
- 2011
- Abstract
- The L1CAM antibody A10-A3 efficiently reduces tumor growth in a nude mouse model. Here, we describe the crystal structure of the Fab fragment of A10-A3 determined at 2.0 angstrom resolution. The A10-A3 antibody H3 loop reveals a characteristic arrangement of exposed aromatic residues that may play an important role in antigen binding. A structure model of the complex between L1CAM Ig1-4 and A10-A3 Fab indicates that the Fab binds to three small loops outside Ig1 and a residue between Ig1 and Ig2, consistent with an epitope mapping result. The data presented here should contribute to the design of high-affinity antibody for therapeutic purposes as well as to the understanding of neural cell remodeling and cancer progression mechanism mediated by L1CAM.
- Keyword
- A10-A3AntibodyCancerCrystal structureL1CAM
- ISSN
- 0014-5793
- Publisher
- Wiley
- DOI
- http://dx.doi.org/10.1016/j.febslet.2010.11.028
- Type
- Article
- Appears in Collections:
- Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
- Files in This Item:
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