Skip to main content
Log in

Solution structure of the recombinant human oncoprotein p13MTCP1

  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

Abstract

The human oncoprotein p13MTCP1 is coded by the MTCP1 gene, a gene involved in chromosomal translocations associated with T-cell prolymphocytic leukemia, a rare form of human leukemia with a mature T-cell phenotype. The primary sequence of p13MTCP1 is highly and only homologous to that of p14TCL1, a product coded by the gene TCL1 which is also involved in T-cell prolymphocytic leukemia. These two proteins probably represent the first members of a new family of oncogenic proteins. We present the three-dimensional solution structure of the recombinant p13MTCP1 determined by homonuclear proton two-dimensional NMR methods at 600 MHz. After proton resonance assignments, a total of 1253 distance restraints and 64 dihedral restraints were collected. The solution structure of p13MTCP1 is presented as a set of 20 DYANA structures. The rmsd values with respect to the mean structure for the backbone and all heavy atoms for the conformer family are 1.07 ± 0.19 and 1.71 ± 0.17 Å, when the structured core of the protein (residues 11–103) is considered. The solution structure of p13MTCP1 consists of an orthogonal β-barrel, composed of eight antiparallel β-strands which present an original arrangement. The two β-pleated loops which emerge from this barrel might constitute the interaction surface with a potential molecular partner.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Banaszak, L., Winter, N., Xu, Z., Bernlohr, D. A., Cowan, S. and Jones, T. A. (1994) In Advances in Protein Chemistry, Vol. 45 (Ed., Schumaker, V.), Academic Press, San Diego, CA, pp. 89–149.

    Google Scholar 

  • Barthe, P., Yang, Y.-S., Chiche, L., Hoh, F., Strub, M.-P., Guignard, L., Soulier, J., Stern, M.-H., van Tilbeurgh, H., Lhoste, J.-M. and Roumestand, C. (1997) J. Mol. Biol., 274, 801–815.

    Google Scholar 

  • Branden, C.-I. and Tooze, J. (1991) An Introduction to Protein Structures, Garland, New York, NY.

    Google Scholar 

  • Braunschweiler, L. and Ernst, R. R. (1983) J. Magn. Reson., 53, 521–528.

    Google Scholar 

  • Chou, K.-C., Heckel, A., Némethy, G., Rumsey, S., Carlacci, L. and Sheraga, H. A. (1990) Proteins, 8, 14–22.

    Google Scholar 

  • Croce, C. M. (1987) Cell, 49, 155–156.

    Google Scholar 

  • Dalhuin, C., Wieruszeski, J. M. and Lippens, G. (1996) J. Magn. Reson., B111, 168–170.

    Google Scholar 

  • Dallapiccola, B., Alimena, G., Chessa, L., Gastaldi, R., De Rossi, G., Semenzato, G., Quinti, I. and Pandolfi, F. (1984) Int. J. Cancer, 34, 171–176.

    Google Scholar 

  • Davey, M. P., Bertness, V., Nakahara, K., Johnson, J. P., McBride, O. W., Waldmann, T. and Kirsch, I. R. (1988) Proc. Natl. Acad. Sci. USA, 85, 9287–9291.

    Google Scholar 

  • Davis, D. G. and Bax, A. (1985) J. Am. Chem. Soc., 107, 2820–2821.

    Google Scholar 

  • Englander, S. W. and Wand, A. J. (1987) Biochemistry, 26, 5958–5962.

    Google Scholar 

  • Fisch, P., Forster, A., Sherrington, P. D., Dyer, M. J. and Rabbit, T. H. (1993) Oncogene, 8, 3271–3276.

    Google Scholar 

  • Fita, I. and Rossmann, M. G. (1985) Proc. Natl. Acad. Sci. USA, 82, 1604–1608.

    Google Scholar 

  • Fu, T.-B., Virgilio, L., Narducci, M. G., Facchiano, A., Russo, G. and Croce, C. M. (1994) Cancer Res., 54, 6297.

    Google Scholar 

  • Goyns, M. H., Hammond, D. W., Harrison, C. J., Menasce, L. P., Ross, F. M. and Hancock, B. W. (1993) Leukemia, 7, 848–852.

    Google Scholar 

  • Güntert, P., Mumenthaler, C. and Wüthrich, K. (1997) J. Mol. Biol., 273, 283–298.

    Google Scholar 

  • Haluska, F. G., Tsujimoto, Y. and Croce, C. M. (1987) Annu Rev. Genet., 21, 321–345.

    Google Scholar 

  • Hendrickson, W. A., Pahler, A., Smith, J. L., Satow, Y., Merritt, E. A. and Phizakerley, R. P. (1989) Proc. Natl. Acad. Sci. USA, 86, 2190–2194.

    Google Scholar 

  • Hyberts, S. G., Märki, W. and Wagner, G. (1987) Eur. J. Biochem., 164, 625–635.

    Google Scholar 

  • Hyberts, S. G., Goldberg, M. S., Havel, T. F. and Wagner, G. (1992) Protein Sci., 1, 736–751.

    Google Scholar 

  • Janin, J. (1996) Prog. Biophys. Mol. Biol., 64, 145–165.

    Google Scholar 

  • Janin, J. (1997) Proteins, 28, 153–161.

    Google Scholar 

  • Janin, J. and Chothia, C. (1990) J. Biol. Chem., 265, 16027–16030.

    Google Scholar 

  • Jeener, J., Meier, B. H., Bachman, P. and Ernst, R. R. (1979) J. Chem. Phys., 71, 4546–4553.

    Google Scholar 

  • Kadkhodaei, M., Hwang, T.-L., Tang, J. and Shaka, A. J. (1993) J. Magn. Reson., A105, 393–399.

    Google Scholar 

  • Karplus, M. (1963) J. Am. Chem. Soc., 85, 2870–2871.

    Google Scholar 

  • Ke, H., Zydowsky, L. D., Liu, J. and Walsh, C. T. (1991) Proc. Natl. Acad. Sci. USA, 88, 9483–9487.

    Google Scholar 

  • Kraulis, P. J. (1991) J. Appl. Crystallogr., 24, 946–950.

    Google Scholar 

  • Kumar, A., Ernst, R. R. and Wüthrich, K. (1980) Biochem. Biophys. Res. Commun., 95, 1–6.

    Google Scholar 

  • Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) J. Appl. Crystallogr., 26, 283–291.

    Google Scholar 

  • Lippens, G., Dhalluin, C. and Wieruszeski, J.-M. (1995) J. Biomol. NMR, 5, 327–331.

    Google Scholar 

  • Ludvigsen, S., Andersen, K. V. and Poulsen, F. M. (1991) J. Mol. Biol., 217, 731–736.

    Google Scholar 

  • Madani, A., Soulier, J., Schmid, M., Plichtova, R., Lermé, F., Gateau-Roesch, O., Garnier, J. P., Pla, M., Sigaux, F. and Stern, M.-H. (1995) Oncogene, 10, 2259–2262.

    Google Scholar 

  • Madani, A., Choukroun, V., Soulier, J., Cacheux, V., Claisse, J. F., Valensi, F., Daliphard, S., Cazin, B., Levy, V., Leblond, V., Daniel, M. T., Sigaux, F. and Stern, M.-H. (1996) Blood, 87, 1923–1927.

    Google Scholar 

  • Marion, D., Ikura, M., Tschudin, R. and Bax, A. (1989) J. Magn. Reson., 85, 393–399.

    Google Scholar 

  • Murzin, A. G., Lesk, A. M. and Chothia, C. (1994a) J. Mol. Biol., 236, 1369–1381.

    Google Scholar 

  • Murzin, A. G., Lesk, A. M. and Chothia, C. (1994b) J. Mol. Biol., 236, 1382–1400.

    Google Scholar 

  • Pardi, A., Billeter, M. and Wüthrich, K. (1984) J. Mol. Biol., 180, 741–751.

    Google Scholar 

  • Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham III, T. E., Fergusson, D. M., Seibel, G. L., Singh, U. C., Weiner, P. K. and Kollman, P. A. (1995) AMBER 4.1, University of California, San Francisco, CA.

    Google Scholar 

  • Piotto, M., Saudek, V. and Sklenar, V. (1992) J. Biomol. NMR, 2, 661–665.

    Google Scholar 

  • Pons, J. L., Malliavin, T. E. and Delsuc, M. A. (1996) J. Biomol. NMR, 8, 445–452.

    Google Scholar 

  • Rabbitts, T. H. (1994) Nature, 372, 143–149.

    Google Scholar 

  • Rance, M., Sørensen, O. W., Bodenhausen, G., Ernst, R. R. and Wüthrich, K. (1983) Biochem. Biophys. Res. Commun., 117, 479–495.

    Google Scholar 

  • Rance, M. (1987) J. Magn. Reson., 74, 557–564.

    Google Scholar 

  • Richardson, J. S. (1981) Adv. Protein Chem., 34, 167–330.

    Google Scholar 

  • Russo, G., Isobe, M., Gatti, R., Finan, J., Batuman, O., Huebner, K., Nowell, P. C. and Croce, C. M. (1989) Proc. Natl. Acad. Sci. USA, 86, 602–606.

    Google Scholar 

  • Sherrington, P. D., Fish, P., Taylor, A. M. R. and Rabbitts, T. H. (1994) Oncogene, 9, 2377–2381.

    Google Scholar 

  • Soulier, J., Madani, A., Cacheux, V., Rosenzwajg, M., Sigaux, F. and Stern, M.-H. (1994) Oncogene, 9, 3565–3570.

    Google Scholar 

  • Stern, M.-H., Soulier, J., Rosenzwajg, M., Nakahara, K., Canki-Klain, N., Aurias, A., Sigaux, F. and Kirsch, I. R. (1993) Oncogene, 8, 2475–2483.

    Google Scholar 

  • Taylor, A. M. R., Metcalfe, J. A., Thick, J. and Mak, Y.-F. (1996) Blood, 87, 423–438.

    Google Scholar 

  • Thick, J., Metcalfe, J. A., Mak, Y.-F., Beatty, D., Minegishi, M., Dyer, M. J. S., Lucas, G. and Taylor, A. M. R. (1996) Oncogene, 12, 379–386.

    Google Scholar 

  • Virgilio, L., Isobe, M., Narducci, M. G., Carotenuto, P., Camerini, B., Kurosawa, N., Abbas-Ar-Rushdi, Croce, C. M. and Russo, G. (1993) Proc. Natl. Acad. Sci. USA, 90, 9275–9279.

    Google Scholar 

  • Wishart, D. S., Sykes, B. D. and Richards, F. M. (1991) J. Mol. Biol., 222, 311–333.

    Google Scholar 

  • Witzig, T. E., Phyliky, R. L., Li, C.-Y., Homburger, H. A., Dewald, G. W. and Handwerger, B. S. (1986) Am. J. Hematol., 21, 139–155.

    Google Scholar 

  • Wüthrich, K., Billeter, M. and Braun, W. (1983) J. Mol. Biol., 169, 949–961.

    Google Scholar 

  • Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York, NY.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yang, YS., Guignard, L., Padilla, A. et al. Solution structure of the recombinant human oncoprotein p13MTCP1 . J Biomol NMR 11, 337–354 (1998). https://doi.org/10.1023/A:1008279616063

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1008279616063

Navigation