정보
Structural insights into FK506 binding proteins, immunophilins w...
Seminar
▶Subject : Structural insights into FK506 binding proteins, immunophilins with versatile biological functions
▶Speaker: Prof. Ho Sup Yoon(Nanyang Technological University)
▶Date : 5:00PM/May.17(Thu)/2012
▶Place : Room 104, Life Science Bldg
*Abstract
Immunophilins are families of proteins interacting with immunosuppressive drugs such as FK506 (tacrolimus), rapamycin (sirolimus), and cyclosporin A. FK506 binding protein (FKBP) family is one of two major immunophilin families and most of FKBP family members bind FK506 and possess peptidylprolyl cis/trans isomerase activity (PPIase). Small FKBP family members contain only FK506-binding domain, while large molecular weight FKBPs possess extra domains such as tetratricopeptide repeat domains, calmodulin binding and transmembrane motifs. The molecular mechanisms of the FKBP family proteins and their cognate ligands in the T-cell activation pathways have been extensively studied. Recent studies prove that immunophilins and their ligands play key roles in cancer, parasite, bacterial and viral infections as well and thus certainly deserve attentions. Despite the well-established molecular mechanism of immunophilins in the T-cell activation pathways, currently, molecular basis of immunophilins and immunophilin-mediated regulatory mechanisms in major biochemical processes such as protein folding, protein-protein interaction and apoptosis still await further studies. To this end, in recent years we’ve been studying some of the FKBP family members including human FKBP38, a noncanonical human FKBP family member, and PfFKBP35 and PvFKPB35, canonical FKBP family members from human malarial parasites Plasmodium falciparum and Plasmodium vivax and AaFKBP12 from Aedes aegypti, a vector for transmitting dengue fever. The molecular characteristics and structural data of those immunophilin members provide insights into the roles of FKBPs across species and also suggest possible routes in designing drugs with novel chemical scaffolds targeting relevant FKBPs to combat cancer, malaria and bacterial infections.
☎ Inquiry :Prof. Kim Kyong Tai (279-2297)
*This Seminar will be given in English