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| [[Image:2eh8.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2eh8.png|left|200px]] |
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| {{STRUCTURE_2eh8| PDB=2eh8 | SCENE= }} | | {{STRUCTURE_2eh8| PDB=2eh8 | SCENE= }} |
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| '''Crystal structure of the complex of humanized KR127 fab and PRES1 peptide epitope'''
| | ===Crystal structure of the complex of humanized KR127 fab and PRES1 peptide epitope=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17517649}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17517649 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17517649}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Neutralization]] | | [[Category: Neutralization]] |
| [[Category: Pres1]] | | [[Category: Pres1]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:33:03 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:59:36 2008'' |