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Title: Backbone 1H, 13C, and 15N resonance assignments of the N-terminal domain of FKBP38 (FKBP38NTD)
Authors: Kang, Cong Bao
Ye, Hong
Vivekanandan, Subramanian
Simon, Bernd
Sattler, Michael
Yoon, Ho Sup
Keywords: DRNTU::Science::Biological sciences::Molecular biology
Issue Date: 2006
Source: Kang, C. B., Ye, H., Vivekanandan, S., Simon, B., Sattler, M., & Yoon, H. S. (2006). Backbone 1H, 13C, and 15N resonance assignments of the N-terminal domain of FKBP38 (FKBP38NTD). Journal of Biomolecular NMR, 36(S1), 37.
Series/Report no.: Journal of biomolecular NMR
Abstract: 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.
DOI: 10.1007/s10858-006-9001-5
Schools: School of Biological Sciences 
Rights: © 2006 Springer. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Biomolecular NMR, Springer. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at:
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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