Human programmed cell death 5 protein has a helical-core and two dissociated structural regions

Biochemical and Biophysical Research Communications

Volumn 318, Issue 2, 2004, Pages 391-396

  Liu, Dongsheng ^a   Feng, Yingang ^a   Cheng, Yuan ^a   Wang, Jinfeng ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Dynamic behavior; Heteronuclear NMR method; Programmed cell death 5; Triple helix bundle

Indexed keywords

NUCLEIC ACID; PROGRAMMED CELL DEATH PROTEIN 5; PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ESCHERICHIA COLI; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; TRIPLE HELIX;

AMINO ACID SEQUENCE; AMINO ACIDS; APOPTOSIS REGULATORY PROTEINS; HUMANS; HYDROPHOBICITY; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT;

ESCHERICHIA COLI;

EID: 2142652103     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.04.044     Document Type: Article

References (19)

1. Liu H., Wang Y., Zhang Y., Song Q., Di C., Chen G., Tang J., Ma D. TFAR19, a novel apoptosis-related gene cloned from human leukemia cell line TF-1, could enhance apoptosis of some tumor cells induced by growth factor withdrawal. Biochem. Biophys. Res. Commun. 254:1999;203-210
2. Rui M., Chen Y., Zhang Y., Ma D. Transfer of anti-TFAR19 monoclonal antibody into HeLa cells by in situ electroporation can inhibit the apoptosis. Life Sci. 71:2002;1771-1778
3. Chen Y., Sun R., Han W., Zhang Y., Song Q., Di C., Ma D. Nuclear translocation of PDCD5 (TFAR19): an early signal for apoptosis? FEBS Lett. 509:2001;191-196
4. Wang Y., Li X., Wang L., Ding P., Zhang Y., Han W., Ma D. An alternative form of paraptosis-like cell death, triggered by TAJ/TROY and enhanced by PDCD5 overexpression. J. Cell Sci. 117:2004;1525-1532
5. ′ -upstream region of human programmed cell death 5 gene contains a highly active TATA-less promoter that is up-regulated by etoposide Gene. 329:2004;39-49
6. Christendat D., Yee A., Dharamsi A., Kluger Y., Savchenko A., Cort J.R., Booth V., Mackereth C.D., Saridakis V., Ekiel I., Kozlov G., Maxwell K.L., Wu N., McIntosh L.P., Gehring K., Kennedy M.A., Davidson A.R., Pai E.F., Gerstein M., Edwards A.M., Arrowsmith C.H. Structural proteomics of an archaeon. Nat. Struct. Biol. 7:2000;903-909
7. Cheng Y., Liu D., Feng Y., Jing G. An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation. Protein Pept. Lett. 10:2003;175-181
8. Cavanagh J., Fairbrother W.J., Palmer A.G., Skelton N.J. Protein NMR Spectroscopy. 1996;Academic Press, San Diego
9. Zhu G., Bax A. Improved linear prediction of damped NMR signals using modified forward back linear prediction. J. Magn. Reson. 100:1992;202-207
10. 15N NMR relaxation. Biochemistry. 33:1994;5984-6003
11. Wishart D.S., Sykes B.D., Richards F.M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1992;1647-1651
12. Schwarzinger S., Kroon G.J., Foss T.R., Chung J., Wright P.E., Dyson H.J. Sequence-dependent correction of random coil NMR chemical shifts. J. Am. Chem. Soc. 123:2001;2970-2978
13. Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132
14. Jones S., Daley D.T., Luscombe N.M., Berman H.M., Thornton J.M. Protein-RNA interactions: a structural analysis. Nucleic Acids Res. 29:2001;943-954
15. Livnah O., Bayer E.A., Wilchek M., Sussman J.L. Three-dimensional structures of avidin and the avidin-biotin complex. Proc. Natl. Acad. Sci. USA. 90:1993;5076-5080
16. Landry S.J., Zeilstra-Ryalls J., Fayet O., Georgopoulos C., Gierasch L.M. Characterization of a functionally important mobile domain of GroES. Nature. 364:1993;255-258
17. Filatov D., Ingemarson R., Graslund A., Thelander L. The role of herpes simplex virus ribonucleotide reductase small subunit carboxyl terminus in subunit interaction and formation of iron-tyrosyl center structure. J. Biol. Chem. 267:1992;15816-15822
18. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680
19. Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics. 15:1999;305-308