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Molecular Modeling Study for Interaction Between urokinase-type Plasminogen Activator and Inhibitor

등록일
2008년 2월 14일 10시 15분 49초
접수번호
1249
발표코드
31P55포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
Liu Shui, 이근우1
경상대학교 응용생명과학부,
1경상대학교 생화학과 응용생명과학부 EB-NCRC,
Tumor cell invasion is a complex, multistep process that involves the controlled degradation of extracellular matrix by tumor cell-associated proteases. Urokinase-type plasminogen activator (uPA), a trypsin like serine protease is strongly associated with tumor cells, flaunts a vital role in several biological processes including tissue remodeling, cell migration, and matrix degradation through a cascade of mechanisms involving activation of zymogen, plasminogen, and the metalloproteases. Thus, it is necessary to develop more potent and selective inhibitors of urokinase as possible cancer therapeutics. In order to investigate the key interaction between urokinase and one of the most active compounds reported by experimental data, molecular dynamics (MD) simulations were performed using GROMACS program. Mutation studies of key residues were carried out to probe the interaction in catalytic site. Besides, the simulation with one inactive compound was also considered to compare with the active one.

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