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A refined structure of human aquaporin‐1
Author(s) -
de Groot Bert L.,
Engel Andreas,
Grubmüller Helmut
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02743-0
Subject(s) - aquaporin , protein structure , chemistry , transporter , water channel , superfamily , crystallography , molecular dynamics , biophysics , biology , biochemistry , gene , computational chemistry , geology , geomorphology , inlet
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 Å 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.