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

Journal of Molecular Biology

Volumn 386, Issue 4, 2009, Pages 1024-1037

  Hemond, Michael ^a   Rothstein, Thomas L ^b   Wagner, Gerhard ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b FEINSTEIN INSTITUTE FOR MEDICAL RESEARCH   (United States)

Author keywords

apoptosis; FAIM; Fas; NMR structure; sandwich

Indexed keywords

CELL PROTEIN; FAS APOPTOSIS INHIBITORY MOLECULE; INHIBITOR PROTEIN; ISOPROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

ANIMALIA; MURINAE;

EID: 60149111590     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.01.004     Document Type: Article

References (26)

1. Schneider T.J., Fischer G.M., Donohoe T.J., Colarusso T.P., and Rothstein T.L. A novel gene coding for a Fas apoptosis inhibitory molecule (FAIM) isolated from inducibly Fas-resistant B lymphocytes. J. Exp. Med. 189 (1999) 949-955
2. Zhong X., Schneider T.J., Cabral D.S., Donohoe T.J., and Rothstein T.L. An alternatively spliced long form of Fas apoptosis inhibitory molecule (FAIM) with tissue-specific expression in the brain. Mol. Immunol. 38 (2001) 62-76
3. Sole C., Dulcet X., Segura M., Gutierrez H., Diaz-Meco M.-T., Gozzelino R., et al. The death receptor agonist FAIM promotes neurite outgrowth by a mechanism that depends on ERK and NF-κB signaling. J. Cell Biol. 167 (2004) 479-492
4. Segura M.F., Sole C., Pascual M., Mubarak R.S., Perez-Garcia M.J., Gozzelino R., et al. The long form of Fas apoptosis inhibitory molecule is expressed specifically in neurons and protects them against death receptor-triggered apoptosis. J. Neurosci. 28 (2007) 11228-11242
5. Wiens M., Perović-Ottstadt S., Müller I.M., and Müller W.E.G. Allograft rejection in the mixed cell reaction system of the desmosponge Suberites domuncula is controlled by differential expression of apoptotic genes. Immunogenetics 56 (2004) 597-610
6. Wiens M., and Müller W.E.G. Cell death in Porifera: molecular players in the game of cell death in living fossils. Can. J. Zool. 84 (2006) 307-321
7. Ito T., and Wagner G. Using codon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of human eIF2α. J. Biol. NMR 28 (2004) 357-367
8. Laskowski R.A., Rullmann J.A.C., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biol. NMR 8 (1996) 477-486
9. Holm L., and Sanders C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
10. Armon A., Grauer D., and Ben-Tal N. ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information. J. Mol. Biol. 307 (2001) 447-463
11. Jones T.A., Bergfors T., Sedzik J., and Unge T. The three-dimensional structure of P2 myelin protein. EMBO J. 7 (1988) 1597-1604
12. Babu Y.S., Bugg C.E., and Cook W.J. Structure of calmodulin refined at 2.2 Angstrom resolution. J. Mol. Biol. 204 (1988) 191-204
13. + conduction and selectivity. Science 280 5360 (1998) 69-77
14. 2O. J. Inorg. Chem. 98 (2003) 161-166
15. Matsudaira P. Sequence from picomolar quantities of protein electroblotted onto polyvinylidene fluoride membrane. J. Biol. Chem. 262 (1987) 10035-10038
16. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
17. Goddard, T. G. & Kneller, D. G. (undated). SPARKY 3. University of California, San Francisco.
18. 13C labeling. Biochemistry 28 (1989) 7510-7516
19. Glc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci. 2 (1993) 543-558
20. Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
21. 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6 (1995) 135-140
22. 7GDP and interaction with 4E-binding protein. Nat. Struct. Biol. 4 (1997) 717-724
23. Dunbrack R.L., and Karplus M. Backbone-dependent rotamer library for proteins: application to side-chain prediction. J. Mol. Biol. 230 (1993) 543-574
24. 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling. J. Am. Chem. Soc. 118 (1996) 6264-6272
25. Cornilescu G., Marquadt J.L., Ottinger M., and Bax A. Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J. Am. Chem. Soc. 120 (1998) 6836-6837
26. Zwecksetter M., and Bax A. Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J. Am. Chem. Soc. 122 (2000) 3791-3792