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

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.