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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Wei CH,Lee ES,Jeon JY,Heo YS,Kim SJ,Jeon YH,Kim KH,Hong HJ,Ryu SE

doi

10.1016/j.febslet.2010.11.028

subject

Has Abstract

pub_date

2011-01-03 00:00:00

pages

153-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(10)00933-6

journal_volume

585

pub_type

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