2EH7: Crystal Structure Of Humanized Kr127 Fab

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)
Humanized Kr127 Fab, Light Chain
Molecule annotation
Humanized Kr127 Fab, Heavy Chain
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB