Functional properties of soybean nodulin 26 from a comparative three-dimensional model.
A model of the nodulin 26 channel protein has been constructed based on comparative modeling and molecular dynamics simulations. Structural features of the protein indicate a selectivity filter that differs from those of the known structures of Escherichia coli glycerol facilitator and mammalian aquaporin 1. The model structure also reveals important roles of Ser207 and Phe96 in ligand binding and transport.
Biswas
Sampa
S
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India. sampa@cmb2.saha.ernet.in
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D020346:Aquaporins / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D008024:Ligands; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010649:Phenylalanine / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000378:metabolism; D013025:Glycine max / Q000737:chemistry*; D055672:Static Electricity
D020346:Aquaporins; D008024:Ligands; D008565:Membrane Proteins; D010940:Plant Proteins; C045625:nodulin; D012694:Serine; D010649:Phenylalanine