2EH7: Crystal Structure Of Humanized Kr127 Fab

Citation:
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.
PDB ID: 2EH7Download
MMDB ID: 61757
PDB Deposition Date: 2007/3/5
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 2EH7: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2EH7
Label Count Molecule
Proteins (2 molecules)
1
Humanized Kr127 Fab, Light Chain
Molecule annotation
1
Humanized Kr127 Fab, Heavy Chain
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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