PDBsum entry 2kd2

Apoptosis

PDB id: 2kd2

Contents

Protein chain

94 a.a.

References listed in PDB file

Key reference

Title

Fas apoptosis inhibitory molecule contains a novel beta-Sandwich in contact with a partially ordered domain.

Authors

M.Hemond, T.L.Rothstein, G.Wagner.

Ref.

J Mol Biol, 2009, 386, 1024-1037. [DOI no: 10.1016/j.jmb.2009.01.004]

PubMed id

19168072

Abstract

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.

Figure 2.
Fig. 2. FAIM-CTD is a noninterleaved β-sandwich. (a) Ribbon diagram of FAIM-CTD, with the N-terminus shown in red. The side chain of the nonnative D148 is also shown. (b) Bundle of 20 structures of FAIM-CTD, colored as in (a). Nine residues preceding K95 are omitted from this figure. (c) Topology diagram of FAIM-CTD. All molecular models were rendered with PyMOL.

Figure 5.
Fig. 5. Structural features of FAIM-CTD. (a) Stick model in stereo of FAIM-CTD, with residues colored as in Fig. 2a, showing cysteine residues 122 and 149. The distance between the two sulfur atoms (purple) in this figure is 8.2 Å. (b) Stick model in stereo of FAIM-CTD, with residues colored according to residue conservation as in Fig. 1e, illustrating the network of hydrophobic contacts involving Trp100, Leu167, Leu102, Val169, and Ile174 that hold together the two β-sheets.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2009, 386, 1024-1037) copyright 2009.