Final report of molecular characterization and regulatory mechanism of immunosuppressant FK506 binding protein 38 (FKBP38) in apoptosis - SEP (Supplementary equipment project RG129/05)

• Main Author: Yoon, Ho Sup.
• Other Authors: School of Biological Sciences
• Format: Research Report
• Language: English
• Published: 2008
• Subjects: DRNTU::Science::Biological sciences::Molecular biology
• Online Access: http://hdl.handle.net/10356/14553
• Institution: Nanyang Technological University

Three-dimensional structural studies revealed that the anti-apoptotic proteins Bcl-2 and Bcl-Xl contains a long loop comprising 50 amino acid residues located between BH4 and the second BH4 regions. This loop has been shown to be unstructured based on NMR or X-ray crystallographic analyses. Recently, this domain has been shown to be regulated at the post-translational levels such as phosphorylation and ubiquitin-dependent degradation, in response to diverse external stimuli such as chemotherapeutic drugs and DNA damages. In most cases, the phosphorylation of Bcl-2 is correlated with the inactivation of Bcl-2 activity. Currently, the mechanism of Bcl-2 phosphorylation remains poorly understand.