Fas Apoptosis Inhibitory Molecule Contains a Novel β-Sandwich in Contact with a Partially Ordered Domain

JOURNAL OF MOLECULAR BIOLOGY

卷:386

Article

Hemond, Michael¹  Rothstein, Thomas L.²  Wagner, Gerhard¹ 

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[2] Feinstein Inst Med Res, Ctr Oncol & Cell Biol, Manhasset, NY 11030 USA

关键词: FAIM;    apoptosis;    Fas;    NMR structure;    beta-sandwich;   

DOI  :  10.1016/j.jmb.2009.01.004

来源: Elsevier

【 摘 要 】

Fas apoptosis inhibitory molecule (FAIM) is a soluble cytosolic protein inhibitor of programmed cell death and is found in organisms throughout the animal kingdom. A short isoform. of FAIM is expressed in all tissue types, while an alternatively spliced long isoform is specifically expressed in the brain. Here, the short isoform is shown to consist of two independently folding domains in contact with each other. The NMR solution structure of the C-terminal domain of murine FAIM is solved in isolation and revealed to be a novel protein fold, a noninterleaved seven-stranded beta-sandwich. The structure and sequence reveal several residues that are likely to be involved in functionally significant interactions with the N-terminal domain or other binding partners. Chemical shift perturbation is used to elucidate contacts made between the N-terminal domain and the C-terminal domain. (C) 2009 Elsevier Ltd. All rights reserved.

【 授权许可】

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