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Structural mechanism of the antigen recognition by the L1 cell adhesion molecule antibody A10-A3 |
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| Authors: | Wei Chun Hua Lee Eung Suk Jeon Jeong Yi Heo Yong-Seok Kim Seung Jun Jeon Young Ho Kim Kyung Hyun Hong Hyo Jeong Ryu Seong Eon |
| Affiliation: | aDepartment of Bio-engineering and Institute for Bioengineering and Biopharmaceutical Research, Hanyang University, Seoul 133-791, Republic of Korea;bDepartment of Bio-analytical Science, University of Science and Technology, Daejeon 305-333, Republic of Korea;cDepartment of System Immunology and Institute of Antibody Research, Kangwon National University, Chuncheon, Kangwon-do 200-701, Republic of Korea;dDepartment of Chemistry, Konkuk University, Seoul 143-701, Republic of Korea;eMedical Proteomics Research Center, KRIBB, Daejeon 305-333, Republic of Korea;fDivision of Magnetic Resonance, Korea Basic Science Institute, Ochang, Chungchungbuk-do 363-883, Republic of Korea;gDepartment of Life Sciences and Biotechnology, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea |
| 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: | Crystal structure Antibody A10-A3 L1CAM Cancer |
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