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Structural mechanism of the antigen recognition by the L1 cell adhesion molecule antibody A10-A3
- 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
- Issue Date
- Jan-2011
- Publisher
- WILEY
- Keywords
- Crystal structure; Antibody; A10-A3; L1CAM; Cancer
- Citation
- FEBS LETTERS, v.585, no.1, pp.153 - 158
- Indexed
- SCIE
SCOPUS
- Journal Title
- FEBS LETTERS
- Volume
- 585
- Number
- 1
- Start Page
- 153
- End Page
- 158
- ISSN
- 0014-5793
- 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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Collections - 서울 공과대학 > 서울 생명공학과 > 1. Journal Articles
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Related Researcher
- Ryu, Seong Eon
- COLLEGE OF ENGINEERING (DEPARTMENT OF BIOENGINEERING)