Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

COMPARATIVE MODELING OF NODULIN 26 FROM GLYCINE MAX.COMPARATIVE MODELING OF NODULIN 26 FROM GLYCINE MAX.

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

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.

Functional properties of soybean nodulin 26 from a comparative three-dimensional model.,Biswas S FEBS Lett. 2004 Jan 30;558(1-3):39-44. PMID:14759513[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Biswas S. Functional properties of soybean nodulin 26 from a comparative three-dimensional model. FEBS Lett. 2004 Jan 30;558(1-3):39-44. PMID:14759513 doi:10.1016/S0014-5793(03)01529-1
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA