Three-dimensional organization of a human water channel

Nature

Volumn 387, Issue 6633, 1997, Pages 627-630

  Cheng, Anchi ^a   Van Hoek, A N ^b,d   Yeager, M ^a,c   Verkman, A S ^b   Mitra, A K ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c SCRIPPS CLINIC   (United States)

^d MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CRYSTALLOGRAPHY; ENDOTHELIUM CELL; GLYCOSYLATION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN TRANSPORT; WATER TRANSPORT;

AQUAPORIN 1; AQUAPORINS; BLOOD GROUP ANTIGENS; CRYSTALLIZATION; FREEZING; HUMANS; IMAGE PROCESSING, COMPUTER-ASSISTED; ION CHANNELS; MODELS, MOLECULAR; PROTEIN CONFORMATION; WATER;

EUKARYOTA; PROKARYOTA;

EID: 0031011374     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/42517     Document Type: Article

References (29)

1. Verkman, A. S. Water Channels (Landes, Austin, TX, 1993).
2. Agre, P., Brown, D. & Nielsen, S. Aquaporin water channels: unanswered questions and unresolved controversies. Curr. Opin. Cell Biol. 7, 472-482 (1995).
3. Zeidel, M. L., Ambudkar, S. V., Smith, B. L. & Agre, P. Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry 31, 7436-7440 (1992).
4. van Hoek, A. N. & Verkman, A. S. Functional reconstitution of the isolated erythrocyte water channel CHIP28. J. Biol. Chem. 267, 18267-18269 (1992).
5. Verkman, A. S. et al. Water transport across mammalian cell membranes. Am. J. Physiol. 270, C12-C30 (1996).
6. Mitra, A. K., Yeager, M., van Hoek, A. N., Wiener, M. C. & Verkman, A. S. Projection structure of the CHIP28 water channel in lipid bilayer membranes at 12-Å resolution. Biochemistry 33, 12735-12740 (1994).
7. Mitra, A. K., van Hoek, A. N., Wiener, M. C., Verkman, A. S. & Yeager, M. The CHIP28 water channel visualized in ice by electron crystallography. Nature Struct. Biol. 2, 726-729 (1995).
8. Jung, J. S., Preston, G. M., Smith, B. L., Guggino, W. B. & Agre, P. Molecular structure of the water channel through aquaporin CHIP: the hourglass model. J. Biol. Chem. 269, 14648-14654 (1994).
9. Denker, B. M., Smith, B. L., Kuhajda, F. P. & Agre, P. Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J. Biol. Chem. 263, 15634-15642 (1988).
10. Walz, T., Typke, D., Smith, B. L., Agre, P. & Engel, A. Projection map of aquaporin-1 determined by electron crystallography. Nature Struct. Biol. 2, 730-732 (1995).
11. 2O-channel, AQP-CHIP, in projection at 3.5 Å resolution. J. Mol. Biol. 251, 413-420 (1995).
12. Henderson, R. & Unwin, P. N. T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257, 28-32 (1975).
13. Kühlbrandt, W. & Wang, D. N. Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature 350, 130-134 (1991).
14. Gorin, M. B., Yancey, S. B. Cline, J., Revel, J.-P. & Horwitz, J. The major intrinsic protein (MIP) of lens fiber membrane. Cell 39, 49-59 (1984).
15. Preston, G. M., Jung, J. S., Guggino, W. B. & Agre, P. Membrane topology of aquaporin CHIP: analysis of functional epitope-scanning mutants by vectorial proteolysis. J. Biol. Chem. 269, 1668-1673 (1994).
16. Chothia, C., Levitt, M. & Richardson, D. Helix to helix packing in proteins. J. Mol. Biol. 145, 215-250 (1981).
17. Walz, T. et al. Surface topographies at subnanometer-resolution reveal asymmetry and sidedness of aquaporin-1. J. Mol. Biol. 264, 907-918 (1996).
18. Park, J. H. & Saier, M. H. Jr. Phylogenetic characterization of the MIP family of transmembrane channel proteins. J. Membr. Biol. 153, 171-180 (1996).
19. Wistow, G. J., Pisano, M. M. & Chepelinsky, A. B. Tandem sequence repeats in transmembrane channel proteins. Trends Biochem. Sci. 16, 170-171 (1991).
20. Smith, B. L. & Agre, P. Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 266, 6407-6415 (1991).
21. Sather, W. A., Yang, J. & Tsien, R. W. Structural basis of ion channel permeation and selectivity. Curr. Opin. Neurobiol. 4, 313-323 (1994).
22. van Hoek, A. N. et al. Purification and structure-function analysis of native, PNGase F-treated and endo-β-galactosidase treated CHIP28 water channels. Biochemistry 34, 2212-2219 (1995).
23. Henderson, R. et al. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213, 899-929 (1990).
24. Agard, D. A. A least squares method for determining structure factors in three-dimensional tilted-view reconstructions. J. Mol. Biol. 167, 849-852 (1983).
25. Unger, V. M. & Schertler, G. F. X. Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68, 1776-1786 (1995).
26. Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M. & Henderson, R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421 (1996).
27. Collaborative Computational Project No. 4. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
28. Upson, C. et al. The application visualization system: A computational environment for scientific visualization. Comput. Graph. Appl. 9, 30-42 (1989).
29. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).