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Title 

Broadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism

Authors 

Seung-Wook ChiC Y MaengSeung Jun KimM S OhC J RyuSang Jick KimKyou Hoon HanHyo Jeong HongSeong Eon Ryu

Publisher 

National Academy of Sciences

Issue Date 

2007

Citation 

Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 22, pp. 9230-9235

Keywords 

alanine-scanning mutagenesiscrystal structurehumanized antibodyvirus neutralizationhepatitis B antibodyimmunoglobulin F(ab) fragmentmonoclonal antibody HxKR127virus proteinantigenantibody affinity

Abstract 

The humanized monoclonal antibody HzKR127 recognizes the preS1 domain of the human hepatitis B virus surface proteins with a broadly neutralizing activity in vivo. We present the crystal structures of HzKR127 Fab and its complex with a major epitope peptide. In the complex structure, the bound peptide forms a type IV β-turn followed by 310 helical turn, the looped-out conformation of which provides a structural basis for broad neutralization. Upon peptide binding, the antibody undergoes a dramatic complementarity determining region H3 lid opening. To understand the structural implication of the virus neutralization, we carried out comprehensive alanine-scanning mutagenesis of all complementarity determining region residues in HzKR127 Fab. The functional mapping of the antigen-combining site demonstrates the specific roles of major binding determinants in antigen binding, contributing to the rational design for maximal humanization and affinity maturation of the antibody.

ISSN 

0027-8424

Link 

http://dx.doi.org/10.1073/pnas.0701279104

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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