The three-dimensional structure of human erythrocyte aquaporin CHIP.

@article{Walz1994TheTS,
  title={The three-dimensional structure of human erythrocyte aquaporin CHIP.},
  author={Thomas Walz and Barbara L Smith and Peter Agre and Andreas H. Engel},
  journal={The EMBO journal},
  year={1994},
  volume={13 13},
  pages={2985-93}
}
Water-permeable membranes of several plant and mammalian tissues contain specific water channel proteins, the 'aquaporins'. The best characterized aquaporin is CHIP, a 28 kDa red blood cell channel-forming integral protein. Isolated CHIP and Escherichia coli lipids may be assembled into 2-D crystals for structural analyses. Here we present (i) a structural characterization of the solubilized CHIP oligomers, (ii) projections of CHIP arrays after negative staining or metal-shadowing, and (iii… CONTINUE READING

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