Structural highlights
4erv is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 4ert, 4ett, 4esu, 4etu, 4etv |
| Gene: | RYR3, HBRR (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[RYR3_HUMAN] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca(2+) release by other calcium channels. Calcium channel that mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. Contributes to cellular calcium ion homeostasis (By similarity). Plays a role in cellular calcium signaling.[1]
Publication Abstract from PubMed
Ryanodine Receptors (RyRs) are huge Ca(2)(+) release channels in the endoplasmic reticulum membrane and form targets for phosphorylation and disease mutations. We present crystal structures of a domain in three RyR isoforms, containing the Ser2843 (RyR1) and Ser2808/Ser2814 (RyR2) phosphorylation sites. The RyR1 domain is the target for 11 disease mutations. Several of these are clustered near the phosphorylation sites, suggesting that phosphorylation and disease mutations may affect the same interface. The L2867G mutation causes a drastic thermal destabilization and aggregation at room temperature. Crystal structures for other disease mutants show that they affect surface properties and intradomain salt bridges. In vitro phosphorylation experiments show that up to five residues in one long loop of RyR2 can be phosphorylated by PKA or CaMKII. Docking into cryo-electron microscopy maps suggests a putative location in the clamp region, implying that mutations and phosphorylation may affect the allosteric motions within this area.
Disease mutations in the ryanodine receptor central region: crystal structures of a phosphorylation hot spot domain.,Yuchi Z, Lau K, Van Petegem F Structure. 2012 Jul 3;20(7):1201-11. Epub 2012 Jun 14. PMID:22705209[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schwarzmann N, Kunerth S, Weber K, Mayr GW, Guse AH. Knock-down of the type 3 ryanodine receptor impairs sustained Ca2+ signaling via the T cell receptor/CD3 complex. J Biol Chem. 2002 Dec 27;277(52):50636-42. Epub 2002 Sep 26. PMID:12354756 doi:http://dx.doi.org/10.1074/jbc.M209061200
- ↑ Yuchi Z, Lau K, Van Petegem F. Disease mutations in the ryanodine receptor central region: crystal structures of a phosphorylation hot spot domain. Structure. 2012 Jul 3;20(7):1201-11. Epub 2012 Jun 14. PMID:22705209 doi:http://dx.doi.org/10.1016/j.str.2012.04.015
