The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable α-helix having unique electrostatic potential character

Biochemical Journal

Volumn 392, Issue 1, 2005, Pages 47-54

  Liu, Dongsheng ^a   Yao, Hongwei ^a   Chen, Yaoyao ^b   Feng, Yingang ^a   Chen, Yingyu ^b   Wang, Jinfeng ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

Author keywords

helix; Apoptosis; Electrostatic potential surface; NMR; Programmed cell death 5 (PDCD5); Solution structure

Indexed keywords

BIOASSAY; DISSOCIATION; ELECTRIC POTENTIAL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

Α-HELIX; APOPTOSIS; ELECTROSTATIC POTENTIAL SURFACE; PROGRAMMED CELL DEATH 5 (PDCD5); SOLUTION STRUCTURE;

CELLS;

PEPTIDE; PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; CELL ACTIVITY; CELL DEATH; CELL STRAIN HL 60; CONTROLLED STUDY; ELECTRICITY; GENE DELETION; HUMAN; HUMAN CELL; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SERUM; SPECTROSCOPY;

AMINO ACID SEQUENCE; APOPTOSIS; APOPTOSIS REGULATORY PROTEINS; ELECTROSTATICS; HL-60 CELLS; HUMANS; MODELS, MOLECULAR; NEOPLASM PROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 28044473860     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050688     Document Type: Article

References (22)

1. Liu, H., Wang, Y., Zhang, Y., Song, Q., Di, C., Chen, G., Tang, J. and Ma, D. (1999) 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, 203-210
2. Chen, Y., Sun, R., Han, W., Zhang, Y., Song, Q., Di, C. and Ma, D. (2001) Nuclear translocation of PDCD5 (TFAR19): an early signal for apoptosis? FEBS Lett. 509, 191-196
3. Wang, Y., Li, X., Wang, L., Ding, P., Zhang, Y., Han, W. and Ma, D. (2004) An alternative form of paraptosis-like cell death, triggered by TAJ/TROY and enhanced by PDCD5 overexpression. J. Cell Sci. 117, 1525-1532
4. Liu, D., Feng, Y., Cheng, Y. and Wang, J. (2004) Human programmed cell death 5 protein has a helical-core and two dissociated structural regions. Biochem. Biophys. Res. Commun. 318, 391-396
5. Christendat, D., Yee, A., Dharamsi, A., Kluger, Y., Savchenko, A., Cort, J. R., Booth, V., Mackereth, C. D., Saridakis, V., Ekiel, I. et al. (2000) Structural proteomics of an archaeon. Nat. Struct. Biol. 7, 903-909
6. Feng, Y. M., Zhang, Y. M. and Jing, G. Z. (2002) Soluble expression in Escherichia coli, purification and characterization of a human TF-1 cell apoptosis-related protein TFAR19. Protein Expression Purif. 25, 323-329
7. Hemsley, A., Arnheim, N., Toney, M. D., Cortopassi, G. and Galas, D. J. (1989) A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res. 17, 6545-6551
8. 15N NMR relaxation. Biochemistry 33, 5984-6003
9. Zhu, G. and Bax, A. (1992) Improved linear prediction of damped NMR signals using modified "forward-backward" linear prediction. J. Magn. Reson. 100, 202-207
10. Cavanagh, J., Fairbrother, W. J., Palmer, A. G. and Skelton, N. J. (1996) Protein NMR Spectroscopy, Academic Press, San Diego
11. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S. et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
12. 13C chemical shifts of amino acids in aqueous solution containing organic solvents: application to the secondary structure characterization of peptides in aqueous trifluoroethanol solution. J. Biomol. NMR 4, 47-59
13. Cornilescu, G., Delaglio, F. and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302
14. Wishart, D. S., Sykes, B. D. and Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333
15. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486
16. Fadok, V. A., Bratton, D. L., Frasch, S. C., Warner, M. L. and Henson, P. M. (1998) The role of phosphatidylserine in recognition of apoptotic cells by phagocytes. Cell Death Differ. 5, 551-562
17. Smith, J. D., Waelde, C., Horwitz, A. and Zheng, P. (2002) Evaluation of the role of phosphatidylserine translocase activity in ABCA1-mediated lipid efflux. J. Biol. Chem. 277, 17797-17803
18. Motta, A., Pastore, A., Goud, N. A. and Castiglione Morelli, M. A. (1991) Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations. Biochemistry 30, 10444-10450
19. Cross, T. A. and Opella, S. J. (1994) Solid-state NMR structural studies of peptides and proteins in membranes. Curr. Opin. Struct. Biol. 4, 574-581
20. Schwarzinger, S., Kroon, G. J., Foss, T. R., Chung, J., Wright, P. E. and Dyson, H. J. (2001) Sequence-dependent correction of random coil NMR chemical shifts. J. Am. Chem. Soc. 123, 2970-2978
21. Wishart, D. S., Sykes, B. D. and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651
22. Koradi, R., Billeter, M. and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55, 29-32