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Title 

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

Authors 

C H WeiE S LeeJ Y JeonY S HeoSeung Jun KimY H JeonK H KimH J HongS E Ryu

Publisher 

Elsevier

Issue Date 

2011

Citation 

FEBS Letters, vol. 585, no. 1, pp. 153-158

Keywords 

A10-A3AntibodyCancerCrystal structureL1CAM

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.

ISSN 

0014-5793

Link 

http://dx.doi.org/10.1016/j.febslet.2010.11.028

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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