Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2

Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2

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. B...

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Main Author: Kang, Congbao
Other Authors: Yoon, Ho Sup
Format: Theses and Dissertations
Published: 2008
Subjects:
DRNTU::Science::Biological sciences::Molecular biology
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-65822020-03-20T21:50:42Z Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2 Kang, Congbao Yoon, Ho Sup School of Biological Sciences DRNTU::Science::Biological sciences::Molecular biology 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. DOCTOR OF PHILOSOPHY (SBS) 2008-09-17T11:42:14Z 2008-09-17T11:42:14Z 2006 2006 Thesis 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. 10356/6582 10.32657/10356/6582 Nanyang Technological University application/pdf
institution Nanyang Technological University
building NTU Library
country Singapore
collection DR-NTU
topic DRNTU::Science::Biological sciences::Molecular biology
spellingShingle DRNTU::Science::Biological sciences::Molecular biology
Kang, Congbao
Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2
description 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.
author2 Yoon, Ho Sup
author_facet Yoon, Ho Sup
Kang, Congbao
format Theses and Dissertations
author Kang, Congbao
author_sort Kang, Congbao
title Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2
title_short Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2
title_full Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2
title_fullStr Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2
title_full_unstemmed Biochemical and structural analysis on the molecular interaction between FK-506 binding protein (FKBP) 38 and anti-apoptotic protein BCL-2
title_sort biochemical and structural analysis on the molecular interaction between fk-506 binding protein (fkbp) 38 and anti-apoptotic protein bcl-2
publishDate 2008
_version_ 1681039970373992448

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