ArticleActa crystallographica. Section F, Structural biology communications2014
Crystallization and preliminary crystallographic analysis of human aquaporin 1 at a resolution of 3.28 Å.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- A conserved H-bond network in human aquaporin-1 is necessary for native folding and oligomerization.Biophysical journal · 2024Article
- Probing the energy barriers and stages of membrane protein unfolding using solid-state NMR spectroscopy.Science advances · 2024Article
- Selective Water Pore Recognition and Transport through Self-Assembled Alkyl-Ureido-Trianglamine Artificial Water Channels.Journal of the American Chemical Society · 2023Article
- Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022Review
- Architecture of the human erythrocyte ankyrin-1 complex.Nature structural & molecular biology · 2022Article
- Aquaporins in the lung.Pflugers Archiv : European journal of physiology · 2019Review
- Aquaporin-graphene interface: relevance to point-of-care device for renal cell carcinoma and desalination.Interface focus · 2018Review
- Structural Basis for Mutations of Human Aquaporins Associated to Genetic Diseases.International journal of molecular sciences · 2018Article
- Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives.Biophysical reviews · 2017Review
- Can Stabilization and Inhibition of Aquaporins Contribute to Future Development of Biomimetic Membranes?Membranes · 2015Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin water channels (AQPs) are found in almost every organism from humans to bacteria. In humans, 13 classes of AQPs control water and glycerol homeostasis. Knockout studies have suggested that modulating the activity of AQPs could be beneficial for the treatment of several pathologies. In particular, aquaporin 1 is a key factor in cell migration and angiogenesis, and constitutes a possible target for anticancer compounds and also for the treatment of glaucoma. Here, a preliminary crystallographic analysis at 3.28 Å resolution of crystals of human aquaporin 1 (hAQP1) obtained from protein expressed in Sf9 insect cells is reported. The crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 89.28, c = 174.9 Å, and contained one monomer per asymmetric unit. The hAQP1 biological tetramer is generated via the crystallographic fourfold axis. This work extends previous electron crystallographic studies that used material extracted from human red blood cells, in which the resolution was limited to approximately 3.8 Å. It will inform efforts to improve lattice contacts and the diffraction limit for the future structure-based discovery of specific hAQP1 inhibitors.
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