File:Figure1 TRPV6 cartoon structure.PNG
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Summary
| Description |
English: Figure 1. Domain organization of TRPV6. TRPV6 monomer contains the following structure elements: an N-terminal helix, an ankyrin repeat domain with six ankyrin repeats (ANK1-6), a linker domain comprised of a β-hairpin (β1 and β2) and two linker helices (LH1 and LH2), a pre-S1 helix connecting the linker domain, and the transmembrane (TM) domain that comprises of six TM helices (S1-S6) and a pore helix connecting S5 and S6, an amphipathic TRP helix, a β-strand forms a β-sheet with β1 and β2, and two C-terminal interacting helices (CIH1 and CIH2). The orientation of the domains is based on that of a cryo-electron microscopy structure of human TRPV6 ((PBD: 6E2F). The positions of the glycosylation site, the key selective residue in the selective filter, a representative residue in the lower gate are also labeled. |
| Source | Own work |
| Author | Vinayakkhattar |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 03:48, 1 August 2020 | | 1,175 × 1,295 (507 KB) | Vinayakkhattar | {{Information |description ={{en|1=Figure 1. Domain organization of TRPV6. TRPV6 monomer contains the following structure elements: an N-terminal helix, an ankyrin repeat domain with six ankyrin repeats (ANK1-6), a linker domain comprised of a β-hairpin (β1 and β2) and two linker helices (LH1 and LH2), a pre-S1 helix connecting the linker domain, and the transmembrane (TM) domain that comprises of six TM helices (S1-S6) and a pore helix connecting S5 and S6, an amphipathic TRP helix, a β-st... |
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