1H6I

A REFINED STRUCTURE OF HUMAN AQUAPORIN 1

Summary for 1H6I

• Entry DOI: 10.2210/pdb1h6i/pdb
• Related: 1FQY 1HW0 1IH5
• Descriptor: AQUAPORIN-1 (1 entity in total)
• Functional Keywords: membrane protein, water channel, two-dimensional crystal
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Membrane; Multi-pass membrane protein: P29972
• Total number of polymer chains: 1
• Total formula weight: 28549.91

Authors

De Groot, B.L.,Engel, A.,Grubmuller, H. (deposition date: 2001-06-15, release date: 2001-12-13, Last modification date: 2024-05-01)

Primary citation

De Groot, B.L.,Engel, A.,Grubmuller, H.
A Refined Structure of Human Aquaporin 1
FEBS Lett., 504:206-, 2001

PubMed Abstract: 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.

PubMed: 11532455
DOI: 10.1016/S0014-5793(01)02743-0

Experimental method

ELECTRON CRYSTALLOGRAPHY (3.54 Å)