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Structural determinants of water permeation through aquaporin-1

Author

Listed:
  • Kazuyoshi Murata

    (National Institute for Physiological Sciences)

  • Kaoru Mitsuoka

    (Faculty of Science, Kyoto University)

  • Teruhisa Hirai

    (Faculty of Science, Kyoto University)

  • Thomas Walz

    (Harvard Medical School)

  • Peter Agre

    (Johns Hopkins University School of Medicine)

  • J. Bernard Heymann

    (M. E. Müller-Institute for Microscopy at the Biozentrum, University of Basel)

  • Andreas Engel

    (M. E. Müller-Institute for Microscopy at the Biozentrum, University of Basel)

  • Yoshinori Fujiyoshi

    (Faculty of Science, Kyoto University)

Abstract

Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8 Å resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 Å over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology—how membranes can be freely permeable to water but impermeable to protons.

Suggested Citation

  • Kazuyoshi Murata & Kaoru Mitsuoka & Teruhisa Hirai & Thomas Walz & Peter Agre & J. Bernard Heymann & Andreas Engel & Yoshinori Fujiyoshi, 2000. "Structural determinants of water permeation through aquaporin-1," Nature, Nature, vol. 407(6804), pages 599-605, October.
    • Handle: RePEc:nat:nature:v:407:y:2000:i:6804:d:10.1038_35036519
    DOI: 10.1038/35036519
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    Citations

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    Cited by:

    1. Zhenyu Yang & Chunyang Yu & Junjie Ding & Lihua Chen & Huiyu Liu & Yangzhi Ye & Pan Li & Jiaolong Chen & Kim Jiayi Wu & Qiang-Yu Zhu & Yu-Quan Zhao & Xiaoning Liu & Xiaodong Zhuang & Shaodong Zhang, 2021. "A class of organic cages featuring twin cavities," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Wanbiao Chen & Rongfeng Zou & Yi Mei & Jiawei Li & Yumi Xuan & Bing Cui & Junjie Zou & Juncheng Wang & Shaoquan Lin & Zhe Zhang & Chongyuan Wang, 2024. "Structural insights into drug transport by an aquaglyceroporin," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    3. Peng Huang & Raminta Venskutonytė & Rashmi B. Prasad & Hamidreza Ardalani & Sofia W. Maré & Xiao Fan & Ping Li & Peter Spégel & Nieng Yan & Pontus Gourdon & Isabella Artner & Karin Lindkvist-Petersso, 2023. "Cryo-EM structure supports a role of AQP7 as a junction protein," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Yasunori Saitoh & Namiki Mitani-Ueno & Keisuke Saito & Kengo Matsuki & Sheng Huang & Lingli Yang & Naoki Yamaji & Hiroshi Ishikita & Jian-Ren Shen & Jian Feng Ma & Michihiro Suga, 2021. "Structural basis for high selectivity of a rice silicon channel Lsi1," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    5. Guangli Liu & Bin Zhou & Jinwei Liu & Huazhang Zhao, 2020. "The Bionic Water Channel of Ultra-Short, High Affinity Carbon Nanotubes with High Water Permeability and Proton Selectivity," Sustainability, MDPI, vol. 13(1), pages 1-13, December.
    6. Lalita Saini & Siva Sankar Nemala & Aparna Rathi & Suvigya Kaushik & Gopinadhan Kalon, 2022. "Selective transport of water molecules through interlayer spaces in graphite," Nature Communications, Nature, vol. 13(1), pages 1-7, December.
    7. Si-Hua Liu & Jun-Hao Zhou & Chunrui Wu & Peng Zhang & Xingzhong Cao & Jian-Ke Sun, 2024. "Sub-8 nm networked cage nanofilm with tunable nanofluidic channels for adaptive sieving," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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