Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
A refined structure of the human water channel aquaporin-1 is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter GlpF, electron crystallographic data at 3.8 A resolution and a multiple sequence alignment of the aquaporin superfamily. The crystallographic R and free R values (36.7% and 37.8%) for the refined structure are significantly lower than for previous models. Improved geometry and enhanced stability in molecular dynamics simulations demonstrate a significant improvement of the aquaporin-1 structure. Comparison with previous aquaporin-1 models shows significant differences, not only in the loop regions, but also in the core of the water channel.
A refined structure of human aquaporin-1.,de Groot BL, Engel A, Grubmuller H FEBS Lett. 2001 Aug 31;504(3):206-11. PMID:11532455[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ de Groot BL, Engel A, Grubmuller H. A refined structure of human aquaporin-1. FEBS Lett. 2001 Aug 31;504(3):206-11. PMID:11532455
