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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2011-1-7
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
3
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pubmed:volume |
585
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
153-8
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pubmed:meshHeading |
pubmed-meshheading:21094640-Amino Acid Sequence,
pubmed-meshheading:21094640-Animals,
pubmed-meshheading:21094640-Antibodies,
pubmed-meshheading:21094640-Antigen-Antibody Complex,
pubmed-meshheading:21094640-Antigens,
pubmed-meshheading:21094640-Binding Sites,
pubmed-meshheading:21094640-Crystallization,
pubmed-meshheading:21094640-Epitope Mapping,
pubmed-meshheading:21094640-Epitopes,
pubmed-meshheading:21094640-HEK293 Cells,
pubmed-meshheading:21094640-Humans,
pubmed-meshheading:21094640-Immunoglobulin Fab Fragments,
pubmed-meshheading:21094640-Mice,
pubmed-meshheading:21094640-Models, Molecular,
pubmed-meshheading:21094640-Neural Cell Adhesion Molecule L1,
pubmed-meshheading:21094640-Protein Binding,
pubmed-meshheading:21094640-Protein Conformation,
pubmed-meshheading:21094640-Protein Structure, Tertiary,
pubmed-meshheading:21094640-X-Ray Diffraction
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pubmed:year |
2011
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pubmed:articleTitle |
Structural mechanism of the antigen recognition by the L1 cell adhesion molecule antibody A10-A3.
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pubmed:affiliation |
Department of Bio-engineering, Hanyang University, Seoul, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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