Structure of RGS4 Bound to AlF4 −-Activated Giα1: Stabilization of the Transition State for GTP Hydrolysis
暂无分享,去创建一个
S. Sprang | A. Gilman | J. Tesmer | Stephen R. Sprang | D. M. Berman | John J.G. Tesmer | David M. Berman | Alfred G. Gilman
[1] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[2] A. Gilman,et al. Synthesis in Escherichia coli of GTPase-deficient mutants of Gs alpha. , 1989, The Journal of biological chemistry.
[3] G. Fasman. Prediction of Protein Structure and the Principles of Protein Conformation , 2012, Springer US.
[4] R. Read. Improved Fourier Coefficients for Maps Using Phases from Partial Structures with Errors , 1986 .
[5] A. Gilman,et al. GAIP and RGS4 Are GTPase-Activating Proteins for the Gi Subfamily of G Protein α Subunits , 1996, Cell.
[6] R. Huber,et al. Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement , 1991 .
[7] S. Sprang,et al. Mechanism of GTP hydrolysis by G-protein alpha subunits. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[8] A. Wittinghofer,et al. Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity , 1992, Molecular and cellular biology.
[9] E. Scolnick,et al. Yeast and mammalian ras proteins have conserved biochemical properties , 1985, Nature.
[10] C Chothia,et al. Surface, subunit interfaces and interior of oligomeric proteins. , 1988, Journal of molecular biology.
[11] A. Brunger. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. , 1992 .
[12] T. Wieland,et al. RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[13] A. Gilman,et al. The GTPase-activating Protein RGS4 Stabilizes the Transition State for Nucleotide Hydrolysis* , 1996, The Journal of Biological Chemistry.
[14] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[15] T. Hunt,et al. RGS10 is a selective activator of Gαi GTPase activity , 1996, Nature.
[16] J. Thorner,et al. RGS Proteins and Signaling by Heterotrimeric G Proteins* , 1997, The Journal of Biological Chemistry.
[17] F. R. Salemme,et al. Structural and functional diversity in 4-α-helical proteins , 1980, Nature.
[18] Axel T. Brunger,et al. X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .
[19] S. Sprang,et al. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. , 1994, Science.
[20] S V Evans,et al. SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. , 1993, Journal of molecular graphics.
[21] A T Brünger,et al. Slow-cooling protocols for crystallographic refinement by simulated annealing. , 1990, Acta crystallographica. Section A, Foundations of crystallography.
[22] S. Sprang,et al. Tertiary and Quaternary Structural Changes in Giα1 Induced by GTP Hydrolysis , 1995, Science.
[23] K. Blumer,et al. RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits , 1996, Nature.
[24] J. Thorner,et al. Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: expression, localization, and genetic interaction and physical association with Gpa1 (the G-protein alpha subunit) , 1996, Molecular and cellular biology.
[25] H. Horvitz,et al. EGL-10 Regulates G Protein Signaling in the C. elegans Nervous System and Shares a Conserved Domain with Many Mammalian Proteins , 1996, Cell.
[26] H. Hamm,et al. Heterotrimeric G proteins. , 1996, Current opinion in cell biology.
[27] H. Hamm,et al. GTPase mechanism of Gproteins from the 1.7-Å crystal structure of transducin α - GDP AIF−4 , 1994, Nature.
[28] S. Sprang,et al. The structure of the G protein heterotrimer Giα1 β 1 γ 2 , 1995, Cell.
[29] H. Bourne,et al. GTPase inhibiting mutations activate the α chain of Gs and stimulate adenylyl cyclase in human pituitary tumours , 1989, Nature.
[30] R. Goody,et al. Formation of a Transition-State Analog of the Ras GTPase Reaction by Ras·GDP, Tetrafluoroaluminate, and GTPase-Activating Proteins , 1996, Science.
[31] E A Merritt,et al. Raster3D Version 2.0. A program for photorealistic molecular graphics. , 1994, Acta crystallographica. Section D, Biological crystallography.
[32] M. Farquhar,et al. GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[33] L. Vallar. GTPase-inhibiting mutations activate the alpha-chain of Gs in human tumours. , 1990, Biochemical Society symposium.
[34] F. McCormick,et al. A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants. , 1987, Science.
[35] A. Warshel,et al. Why have mutagenesis studies not located the general base in ras p21 , 1994, Nature Structural Biology.
[36] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[37] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[38] S H Kim,et al. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. , 1992, Science.
[39] S. Harrison,et al. Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[40] S. Kim,et al. X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[41] S. Smerdon,et al. The structure of the GTPase-activating domain from p50rhoGAP , 1997, Nature.
[42] E. Neer. Heterotrimeric C proteins: Organizers of transmembrane signals , 1995, Cell.
[43] W. Kabsch,et al. Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras , 1996, Nature.
[44] F. Bischoff,et al. Structural Differences in the Minimal Catalytic Domains of the GTPase-activating Proteins p120GAP and Neurofibromin* , 1996, The Journal of Biological Chemistry.
[45] A. Gilman,et al. RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[46] B. Lee,et al. The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.
[47] R. K. Chan,et al. Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and alpha factor pheromones , 1982, Molecular and cellular biology.
[48] H. Hamm,et al. The 2.0 Å crystal structure of a heterotrimeric G protein , 1996, Nature.
[49] K. Blumer,et al. Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family , 1996, Nature.
[50] A. Gilman,et al. G proteins: transducers of receptor-generated signals. , 1987, Annual review of biochemistry.
[51] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[52] A. Gilman,et al. Mutations of GS alpha designed to alter the reactivity of the protein with bacterial toxins. Substitutions at ARG187 result in loss of GTPase activity. , 1989, The Journal of biological chemistry.
[53] G. N. Ramachandran,et al. Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.
[54] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[55] A. Gilman,et al. Expression of G-protein alpha subunits in Escherichia coli. , 1994, Methods in enzymology.
[56] J. Thompson,et al. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. , 1994, Nucleic acids research.
[57] V. Arshavsky,et al. Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP , 1992, Nature.
[58] J. Richardson,et al. Principles and Patterns of Protein Conformation , 1989 .
[59] Bruce R. Conklin,et al. Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors , 1993, Cell.
[60] E. Ross. G protein GTPase-activating proteins: regulation of speed, amplitude, and signaling selectivity. , 1995, Recent progress in hormone research.
[61] S. Sprang,et al. Structure of the GDP–Pi complex of Gly203→Ala Giα1: a mimic of the ternary product complex of Gα-catalyzed GTP hydrolysis , 1996 .