journal menu
![[Figure 9]](lv5073fig9mag.jpg)
|
|
Figure 9
The hRyR21–606 homology model docked into a cryo-EM map of the closed RyR1 (EMD 1606). (a, b) Side view of residues 5–10 (blue) and 342–352 (green) of a single monomer (a) and residues 1–12 (blue) and 336–342 (green) of two neighbouring monomers (b) pointing into the channel pore; (c) oblique view of the flexible loop (amino acids 377–387, green); (d) top view of the C-terminus (amino acids 545–606, red) containing the LIZ motif (amino acids 555–586) with the amino acids (L565EASSGIL) that interact with spinophilin shown in orange. (e) Oblique view of the above LIZ motif with attached complex of spinophilin (PDB entry 3egg chain C, pink; L492ELFPVEL, purple) with PP1 (PDB entry 3egg chain A, green). Domains A and C of hRyR21–606 are shown in blue and red, respectively. RyR1 cryo-EM map regions are numbered according to Serysheva et al. (2008  ). In (a)–(e) the structural detail is shown in the left panel; a view of the whole RyR2 from the same angle is shown in the right panel. The rectangle corresponds to the area shown in the left panel. |
![[Figure 9]](lv5073fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
