| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871963 | FEBS Letters | 2011 | 6 Pages |
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.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Chun Hua Wei, Eung Suk Lee, Jeong Yi Jeon, Yong-Seok Heo, Seung Jun Kim, Young Ho Jeon, Kyung Hyun Kim, Hyo Jeong Hong, Seong Eon Ryu,