Structure of a voltage-dependent K+ channel β subunit

Cell

Volumn 97, Issue 7, 1999, Pages 943-952

  Gulbis, Jacqueline M ^a   Mann, Sabine ^a   MacKinnon, Roderick ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE; POTASSIUM CHANNEL;

ARTICLE; CHANNEL GATING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBUNIT; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

MAMMALIA;

EID: 0033603236     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80805-3     Document Type: Article

References (46)

1. Alber, T., Banner, D.W., Bloomer, A.C., Petsko, G.A., Phillips, D., Rivers, P.S., and Wilson, I.A. (1981). On the three-dimensional structure and catalytic mechanism of those phosphate isomerase. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 293, 159-171.
2. Altschul, S.F., Gish, W., Miller, W., Myers, E.W., and Lipman, D.J. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
3. Bacon, D., and Anderson, W.F. (1988). A fast algorithm for rendering space filling molecule pictures. J. Mol. Graph. 6, 219-220.
4. Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
5. Benner, S.A. (1982). The stereoselectivity of alcohol dehydrogenases: a stereochemical imperative? Experientia 38, 633-637.
6. Bennett, M.J., Albert, R.H, Jez, J.M., Ma, H., Penning, T.M., and Lewis, M. (1997). Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase. Structure 5, 799-812.
7. Bohren, K.M., Grimshaw, C.E., Lai, C.-J., Harrison, D.H., Ringe, D., Petsko, G.A., and Gabbay, K.H. (1994). Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 33, 2021-2032.
8. Borhani, D.W., Harter, T.M., and Petrash, J.M. (1992). The crystal structure of the aldose reductase. NADPH binary complex. J. Biol. Chem. 267, 24841-24847.
9. Branden, C., and Tooze, J. (1999). Introduction to Protein Structure (New York: Garland Publishing, Inc.).
10. Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kuntsleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. (1998). Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921.
11. CCP4. (1994). Programs for X-ray crystallography. Acta Crystallogr. D 50, 760-763.
12. Chouinard, S.W., Wilson, G.F., Schlimgen, A.K., and Ganetzky, B. (1995). A potassium channel beta subunit related to the aldo-keto reductase superfamily is encoded by the Drosophila hyperkinetic locus. Proc. Natl. Acad. Sci. USA 92, 6763-6767.
13. + conduction and selectivity. Science 280, 69-77.
14. El-kabbani, O., Judge, K., Ginell, S.L, Myles, D.A., DeLucas, L.J., and Flynn, T.G. (1995). Structure of porcine aldehyde reductase holoenzyme. Nat. Struct. Biol. 2, 687-692.
15. Harrison, D.H., Bohren, K.M., Ringe, D., Petsko, G.A., and Gabbay, K.H. (1994). An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate. Biochemistry 33, 2011-2020.
16. Heinemann, S.H., Rettig, J., Graack, H.R., and Pongs, O. (1996). Functional characterization of Kv channel beta-subunits from rat brain. J. Physiol. 493, 625-633.
17. Hille, B. (1992). Ionic Channels of Excitable Membranes (Sunderland, MA: Sinauer Associates, Inc.).
18. Holm, L., and Sander, C. (1998). Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26, 316-319.
19. Hoshi, T., Zagotta, W.N., and Aldrich, R.W. (1990). Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250, 533-538.
20. Ireland, L.S., Harrison, D.J., Neal, G.E., and Hayes, J.D. (1998). Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase. Biochem. J. 332, 21-34.
21. Jez, J.M., Flynn, T.G., and Penning, T.M. (1997). A new nomenclature for the aldo-keto reductase superfamily. Biochem. Pharmacol. 54, 639-647.
22. Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
23. Kaplan, W.D., and Trout W.E., III. (1969). The behavior of four neurological mutants of Drosophila. Genetics 61, 399-409.
24. Kleywegt, G.J., and Jones, T.A. (1994). From the first map to final model. In Proceedings of the CCP4 Study Weekend, S. Bailey, R. Hubbard, and D. Waller, eds. (Daresbury, UK: Daresbury Laboratory), pp. 59-66.
25. Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
26. Kreusch, A., Pfaffinger, P.J., Stevens, C.F., and Choe, S. (1998). Crystal structure of the tetramerization domain of the Shaker potassium channel. Nature 392, 945-948.
27. Livingston, C.D., and Barton, G.J. (1993). Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation. Comput. Appl. Biosci. 9, 745-756.
28. + channel beta subunits belong to an NAD(P)H-dependent oxidoreductase superfamily. Cell 79, 1133-1135.
29. McCormack, K., McCormack, T., Tanouye, M., Rudy, B., and Stuhmer, W. (1995). Alternative splicing of the human Shaker K channel beta 1 gene and functional expression of the beta 2 gene product. FEBS Lett. 370, 32-36.
30. Nagaya, N., and Papazian, D.M. (1997). Potassium channel alpha and beta subunits assemble in the endoplasmic reticulum. J. Biol. Chem. 272, 3022-3027.
31. Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
32. Otwinowski, Z. (1993). Data collection and processing. In Proceedings of the CCP4 Study Weekend, L. Sawyer, N. Isaac, and S. Bailey, eds. (Daresbury, UK: Daresbury Laboratory), pp. 56-62.
33. Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
34. Parcej, D.N., Scott, V.E.S., and Dolly, J.O. (1992). Oligomeric properties of alpha-dendrotoxin-sensitive potassium ion channels purified from bovine brain. Biochemistry 31, 11084-11088.
35. Pawlowski, J.E., and Penning, T.M. (1994). Overexpression and mutagenesis of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. J. Biol. Chem. 269, 13502-13510.
36. 2 sensitivity to Kv4.2 but not to Shaker channels. J. Gen. Physiol. 113, 897-907.
37. +-channel protein identified by its binding properties for dendrotoxin I. Proc. Natl. Acad. Sci. USA 85, 4919-4923.
38. + channels altered by presence of beta-subunit. Nature 369, 289-294.
39. + channels from bovine brain. Proc. Natl. Acad. Sci. USA 91, 1637-1641.
40. + channel surface expression through effects early in biosynthesis. Neuron 16, 843-852.
41. + channel through multiple binding sites. Neuron 18, 665-673.
42. Tang, H., Vasconcelos, A.C., and Berkowitz, G.A. (1996). Physical association of KAB1 with plant K channel alpha subunits. Plant Cell 8, 1545-1553.
43. Tempel, B.L., Papazian, D.M., Schwarz, T.L., Jan, Y.N., and Jan, L.Y. (1987). Sequence of a probable potassium channel component encoded at Shaker locus of Drosophila. Science 237, 770-775.
44. Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
45. Wilson, D.K., Bohren, K.M., Gabbay, K.H., and Quiocho, F.A. (1992). An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257, 81-84.
46. + channels in transfected mammalian cells. J. Biol. Chem. 272, 11728-11735.