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. Author manuscript; available in PMC: 2015 Jan 1.
Published in final edited form as: Pflugers Arch. 2013 Oct 6;466(1):10.1007/s00424-013-1370-5. doi: 10.1007/s00424-013-1370-5

Figure 2. Structure of the core of human NKCC1.

Figure 2

A) Structure of the transmembrane domains and other alpha helices was modeled using the Phyre2 protein fold recognition server [72]. The PDB file was viewed using the Visual Molecular Dynamics software (University of Illinois) and the image was rendered after highlighting the alpha helices. The first 5 TMs are colored in blue, whereas the next five TMs are colored in red. Note the proximity and parallelism of TM1-6, TM2-7, TM3-8, and TM4-9. B) Predicted topology of the first 10 transmembrane domains based on similarity to crystal structure of amino acid-polyamine-organocation transporters. The last 2 transmembrane domains are not drawn. C. Alignment of two segments of the human NKCC1 core showing conservation of transmembrane domains. The SV and MM/VV amino acids in human NKCC1 TMD2-7 are replaced by AL and GT in shark NKCC1. The alignment was done with VectorNti 6 (Invitrogen).