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Structural mechanism of the antigen recognition by the L1 cell adhesion molecule antibody A10-A3

Authors
Wei, Chun HuaLee, Eung SukJeon, Jeong YiHeo, Yong-SeokKim, Seung JunJeon, Young HoKim, Kyung HyunHong, Hyo JeongRyu, Seong Eon
Issue Date
3-1월-2011
Publisher
ELSEVIER SCIENCE BV
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
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/113290
DOI
10.1016/j.febslet.2010.11.028
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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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약학대학 (약학과)
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