Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/6582
Title: Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2
Authors: Kang, Congbao
Keywords: DRNTU::Science::Biological sciences::Molecular biology
Issue Date: 2006
Source: Kang, C. B. (2006). Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2. Doctoral thesis, Nanyang Technological University, Singapore.
Abstract: FK506 binding protein (FKBP) 38, which is a tripartite TPR domain-containing member in the FKBP family, can help Bcl-2 localize at the mitochondrial membrane and modulate apoptosis. The regulation of Bcl-2 function by forming heterodimeric complexes with its pro-apoptotic partners is well studied. Bcl-2 is also regulated at the posttranslational level through phosphorylation of specific residues within the flexible loop. Bcl-2 contains an unusually long loop between the first and the second helices. This loop has been shown to be highly flexible based on NMR and X-ray crystallographic analyses of this region. Currently, the molecular basis of alternative regulatory mechanism of Bcl-2 remains poorly understood.
URI: https://hdl.handle.net/10356/6582
DOI: 10.32657/10356/6582
Rights: Nanyang Technological University
Fulltext Permission: open
Fulltext Availability: With Fulltext
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