2EH7

Crystal structure of humanized KR127 FAB

Summary for 2EH7

• Entry DOI: 10.2210/pdb2eh7/pdb
• Related: 2EH8
• Descriptor: HUMANIZED KR127 FAB, LIGHT CHAIN, HUMANIZED KR127 FAB, HEAVY CHAIN (2 entities in total)
• Functional Keywords: hepatitis b virus, humanized antibody, monoclonal antibody, neutralization, pres1, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 46978.49

Authors

Chi, S.-W.,Kim, S.-J.,Maeng, C.-Y.,Hong, H.J.,Ryu, S.-E. (deposition date: 2007-03-05, release date: 2008-01-15, Last modification date: 2024-10-09)

Primary citation

Chi, S.-W.,Maeng, C.-Y.,Kim, S.J.,Oh, M.S.,Ryu, C.J.,Kim, S.-J.,Han, K.-H.,Hong, H.J.,Ryu, S.-E.
Broadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism
Proc.Natl.Acad.Sci.Usa, 104:9230-9235, 2007

PubMed 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 beta-turn followed by 3(10) 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.

PubMed: 17517649
DOI: 10.1073/pnas.0701279104

Experimental method

X-RAY DIFFRACTION (2.5 Å)