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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Structure of the anti-HBV antibody-antigen complex

등록일
2008년 8월 21일 19시 55분 35초
접수번호
1574
발표코드
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발표시간
금 15시 : 30분
발표형식
심포지엄
발표분야
생명화학 - Omics & Personalized Medicine II
저자 및
공동저자
류성언
한국생명공학연구원 단백체시스템연구단, Korea
Human hepatitis B virus (HBV) is a small enveloped DNA virus, which causes acute and chronic hepatitis in humans. There are about 400 million carriers of HBV worldwide, providing a serious threat to people’s health. The current HBV vaccines have several limitations including non-responsiveness, escape mutants, and low immunogenicity. To shed light on the antigen recognition mechanism of the broadly neutralizing antibody of HBV, we determined the crystal structures of antibody HzKR127 in its free and antigen peptide-bound forms. In the complex structure, the bound peptide forms a type IV beta-turn followed by 3-10 helical turn, whose looped-out conformation provides a structural basis for broad neutralization. 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.

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