Crystal structure of human Rad GTPase of the RGK-family

Genes to Cells

Volumn 11, Issue 8, 2006, Pages 961-968

  Yanuar, Arry ^a   Sakurai, Shigeru ^a   Kitano, Ken ^a   Hakoshima, Toshio ^a,b  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCINE; GUANINE; GUANOSINE TRIPHOSPHATASE; MAGNESIUM ION; PHENYLALANINE; PROTEIN RAD; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENE SWITCHING; GENETIC CONSERVATION; HUMAN; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; GTP PHOSPHOHYDROLASES; GUANOSINE DIPHOSPHATE; HUMANS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PHOSPHATE-BINDING PROTEINS; PHOSPHATES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RAS PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 33746178724     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2006.00994.x     Document Type: Article

References (30)

1. 2+ channel regulation. J. Mol. Biol. 355, 34-46.
2. 2+ channel expression at the cell surface by the small G-protein kir/Gem. Nature 411, 701-706.
3. Brünger, A.T., Adams, P.D., Clore, G.M., et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921.
4. CCP4 (Collaborative Computational Project, Number, 4). (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
5. Cohen, L., Mohr, R., Chen, Y.Y., et al. (1994) Transcriptional activation of a ras-like gene (kir) by oncogenic tyrosine kinases. Proc. Natl. Acad. Sci. USA 91, 12448-12452.
6. DeLano, W.L. & Bromberg, S. (2004) Pymol. User's Guide (http://www.pymol.org/), San Carlos, California: DeLano Scientific LLC.
7. Finlin, B.S., Crump, S.M., Satin, J. & Andres, D.A. (2003) Regulation of voltage-gated calcium channel activity by the Rem and Rad GTPases. Proc. Natl. Acad. Sci. USA 100, 14469-14474.
8. Hakoshima, T., Shimizu, T. & Maesaki, R. (2003) Structural basis of the Rho GTPase signaling. J. Biochem. (Tokyo) 134, 327-331.
9. Ihara, K., Muraguchi, S., Kato, M., et al. (1998) Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J. Biol. Chem. 273, 9656-9666.
10. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A Found. Crystallogr. 47, 110-119.
11. Kelly, K. (2005) The RGK family: A regulatory tail of small GTP-binding proteins. Trends Cell Biol. 15, 640-643.
12. Krengel, U., Schlichting, L., Scherer, A., et al. (1990) Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules. Cell 62, 539-548.
13. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26, 283-291.
14. Moyers, J.S., Bilan, P.J., Reynet, C. & Kahn, C.R. (1996) Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells. J. Biol. Chem. 271, 23111-23116.
15. Moyers, J.S., Bilan, P.J., Zhu, J. & Kahn, C.R. (1997) Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II. J. Biol. Chem. 272, 11832-11839.
16. Nicely, N.I., Kosak, J., de Serrano, V. & Mattos, C. (2004) Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap. Structure 12, 2025-2036.
17. Olson, M.F. (2002) Gem GTPase: Between a ROCK and a hard place. Curr. Biol. 12, R496-R498.
18. Otwinowski, Z. & Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
19. Pai, E.F., Krengel, U., Petsko, G.A., Goody, R.S., Kabsch, W. & Wittinghofer, A. (1990) Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Åresolution: Implications for the mechanism of GTP hydrolysis. EMBO J. 9, 2351-2359.
20. Reynet, C. & Kahn, C.R. (1993) Rad: A member of the Ras family overexpressed in muscle of type II diabetic humans. Science 262, 1441-1444.
21. Sali, A. & Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
22. Takai, Y., Sasaki, T. & Matozaki, T. (2001) Small GTP-binding proteins. Physiol. Rev. 81, 153-208.
23. Terwilliger, T.C. (2003) Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. D Biol. Crystallogr. 59, 38-44.
24. Tong, L.A., de Vos, A.M., Milburn, M.V. & Kim, S.H. (1991) Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J. Mol. Biol. 217, 503-516.
25. Tseng, Y.H., Vicent, D., Zhu, J., et al. (2001) Regulation of growth and tumorigenicity of breast cancer cells by the low molecular weight GTPase Rad and nm23. Cancer Res. 61, 2071-2079.
26. Vetter, I.R. & Wittinghofer, A. (2001) The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304.
27. Ward, Y., Yap, S.F., Ravichandran, V., et al. (2002) The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway. J. Cell Biol. 157, 291-302.
28. Yanuar, A., Sakurai, S., Kitano, K. & Hakoshima, T. (2005) Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase. Acta Crystallogr. F Struct. Biol. Cryst. Commun. 61, 978-980.
29. Zhu, J., Reynet, C., Caldwell, J.S. & Kahn, C.R. (1995) Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity. J. Biol. Chem. 270, 4805-4812.
30. Zhu, J., Tseng, Y.H., Kantor, J.D., et al. (1999) Interaction of the Ras-related protein associated with diabetes rad and the putative tumor metastasis suppressor NM23 provides a novel mechanism of GTPase regulation. Proc. Natl. Acad. Sci. USA 96, 14911-14918.