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.
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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 |
Journal | FEBS letters
(FEBS Lett)
Vol. 585
Issue 1
Pg. 153-8
(Jan 03 2011)
ISSN: 1873-3468 [Electronic] England |
PMID | 21094640
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
Chemical References |
- Antibodies
- Antigen-Antibody Complex
- Antigens
- Epitopes
- Immunoglobulin Fab Fragments
- Neural Cell Adhesion Molecule L1
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Topics |
- Amino Acid Sequence
- Animals
- Antibodies
(chemistry, immunology, metabolism)
- Antigen-Antibody Complex
(chemistry, immunology, metabolism)
- Antigens
(chemistry, immunology, metabolism)
- Binding Sites
- Crystallization
- Epitope Mapping
- Epitopes
(chemistry, immunology, metabolism)
- HEK293 Cells
- Humans
- Immunoglobulin Fab Fragments
(chemistry, immunology, metabolism)
- Mice
- Models, Molecular
- Neural Cell Adhesion Molecule L1
(chemistry, immunology, metabolism)
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary
- X-Ray Diffraction
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