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|
| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Event Hall |
| Time |
4월 20일 (금요일) 11:00~12:30 |
| Code |
BIO.P-304 |
| Subject |
Bio-techniques for mass production of secreted N-and O-gly-deficient αVβ3 ectodomain |
| Authors |
Bok-Soo Lee, Yong Ho Kim1,*
Sungkyunkwan University, Korea
1Department of Chemistry, SKKU Advanced Institute o, Sungkyunkwan University, Korea
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| Abstract |
Helicobacter pylori(Hp) initialize its pathogenicity by attaching to host cell membrane using its own secretion system, called T4SS pili. HpT4SS consists of CagL proteins and succeeds in binding a RGD sequence of CagL protein to integrin in gastric epithelial cell. A canonical RGD sequences flexible and known to interact with ectodomain of integrins. However, several studies recently claimed that neighboring sequences around RGD motif is also important for the interaction, indicating that an RGD motif may not be necessary for the integrin binding. Furthermore, recent crystal structure of CagLK74revealed that RGD motif positioned surprisingly in the middle of long-rigid a-helix, implying that a canonical RGD sequence may not be essential for integrin binding. Therefore, the structural study of CagLK74- integrin complex could elucidate the precise mechanism of the interaction, which, in turn, provide basic knowledge for the development of drugs preventing gastric cancer and ulcer. A prerequisite for the study is to obtain integrin protein with high purity and amounts. Here, we established the stable expression of genetically-engineered aVb3 ectodomain without post-translational modification, which will enable us to determine CagL-aVb3 complex structure. |
| E-mail |
bslee114@gmail.com |
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121st General Meeting of the KCS