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![[Figure 5]](lv5073fig5mag.jpg)
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Figure 5
Conformation of residues at the putative binding sites of RyR2. (a) A stereoview of the salt-bridge/hydrogen-bond network of hRyR21–606 stabilizing the A/B/C interface. Hydrogen bonds are shown as dashed lines. (b) A stereoview of the superposition of the chloride-binding site of mRyR21–547 (light beige) with the equivalent site of hRyR21–606. There are major differences in the conformations of the Glu40, Tyr125, Arg276 and Arg417 side chains; the mRyR21–547 chloride anion (indicated) has no equivalent in the hRyR21–606 structure. (c, d) Comparison of the hRyR21–606 structure close to the A/C interface (c) and the A/B/C interface (d) with the putative PEG binding sites of the mRyR21–547 structure. In the 4jqk structure, the Phe42 side chain is located in one of the PEG binding sites found in mRyR21–547 (c). In the region of the other putative PEG binding site, no electron density is present in 4jkq except for a single water molecule (d). Residues from domains A, B and C of hRyR21–606 are shown in blue, green and red, respectively. Residues of mRyR21–547 are shown in light beige. PEG is coloured in grey. Electron density is drawn at the 1σ level. This figure was prepared with PyMOL (Schrödinger). |
![[Figure 5]](lv5073fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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