Journal
FEBS LETTERS
Volume 585, Issue 1, Pages 153-158Publisher
WILEY
DOI: 10.1016/j.febslet.2010.11.028
Keywords
Crystal structure; Antibody; A10-A3; L1CAM; Cancer
Funding
- Hanyang University
- Ministry of Science and Technology (Korea) [C1007150-01-01]
- Kangwon National University
- KRIBB
- NMR Research Program of KBSI
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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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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