Backbone 1H, 13C, and 15N resonance assignments of the N-terminal domain of FKBP38 (FKBP38NTD)

• Main Authors: Kang, Cong Bao, Ye, Hong, Vivekanandan, Subramanian, Simon, Bernd, Sattler, Michael, Yoon, Ho Sup
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2012
• Subjects: DRNTU::Science::Biological sciences::Molecular biology
• Online Access: https://hdl.handle.net/10356/79968; http://hdl.handle.net/10220/8826
• Institution: Nanyang Technological University

FK-506 binding protein 38 (FKBP38) interacts with Bcl-2/Bcl-Xl and helps them localize at the mitochondrial membrane (Shirane and Nakayama, 2003). The down-regulation of FKBP38 was shown to influence on the stability of Bcl-2 and consequently induce apoptotic cell death (Kang et al., 2005). FKBP38 is a unique protein among the FKBP family members. Unlike other members in the FKBP family, FKBP38 appears to have no FK-506 binding activity (Shirane and Nakayama, 2003). Thus, to understand the function of FKBP38 at molecular level, as the first step, we performed a NMR study on FKBP38, and here we report the NMR resonance assignments of the N-terminal domain of FKBP38, which includes the FK-506 binding domain and the flanking N-terminal residues. Nearly all of the backbone 1H, 13C, and 15N resonances were assigned ( 99%). Assignments of the side chain atoms beyond Cβ atoms are about 80% complete. The assignments have been deposited with BMRB accession number 6923.