3rqr

From Proteopedia

(Difference between revisions)

Revision as of 15:04, 24 December 2014

Crystal structure of the RYR domain of the rabbit ryanodine receptor

Structural highlights

3rqr is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	RYR1 (Oryctolagus cuniculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[RYR1_RABIT] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity).^[1] ^[2]

Publication Abstract from PubMed

The ryanodine receptor (RyR) is a large, homotetrameric sarcoplasmic reticulum (SR) membrane protein essential for Ca(2+) cycling in both skeletal and cardiac muscle. Genetic mutations in RyR1 are associated with severe conditions including malignant hyperthermia (MH) and central core disease (CCD). One phosphorylation site (Ser 2843) has been identified in a segment of RyR1 flanked by two RyR motifs, which are found exclusively in all RyR isoforms organized as closely-associated tandem (or paired) motifs, and named after the protein itself. These motifs also contain six known MH mutations. In this study we designed, expressed, and purified the tandem RyR motifs and show that this domain contains a putative binding site for the Ca(2+) /calmodulin-dependent protein kinase beta isoform. We present a 2.2A resolution crystal structure of the RyR domain revealing a two-fold, symmetric, extended four-helix bundle stabilized by a beta-sheet. Using mathematical modelling we fit our crystal structure within a tetrameric EM structure of native RyR1 and propose that this domain is localized in the RyR's clamp region, which is absent in its cousin protein inositol 1,4,5-trisphosphate receptor. (c) 2012 The Authors Journal compilation (c) 2012 FEBS.

Structural Determination of the Phosphorylation Domain of the Ryanodine Receptor.,Sharma P, Ishiyama N, Nair U, Li W, Dong A, Miyake T, Wilson A, Ryan T, Maclennan DH, Kislinger T, Ikura M, Dhe-Paganon S, Gramolini AO FEBS J. 2012 Aug 22. doi: 10.1111/j.1742-4658.2012.08755.x. PMID:22913516^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dulhunty AF, Laver DR, Gallant EM, Casarotto MG, Pace SM, Curtis S. Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12. Biophys J. 1999 Jul;77(1):189-203. PMID:10388749 doi:10.1016/S0006-3495(99)76881-5
↑ Kakizawa S, Yamazawa T, Chen Y, Ito A, Murayama T, Oyamada H, Kurebayashi N, Sato O, Watanabe M, Mori N, Oguchi K, Sakurai T, Takeshima H, Saito N, Iino M. Nitric oxide-induced calcium release via ryanodine receptors regulates neuronal function. EMBO J. 2011 Oct 28;31(2):417-28. doi: 10.1038/emboj.2011.386. PMID:22036948 doi:10.1038/emboj.2011.386
↑ Sharma P, Ishiyama N, Nair U, Li W, Dong A, Miyake T, Wilson A, Ryan T, Maclennan DH, Kislinger T, Ikura M, Dhe-Paganon S, Gramolini AO. Structural Determination of the Phosphorylation Domain of the Ryanodine Receptor. FEBS J. 2012 Aug 22. doi: 10.1111/j.1742-4658.2012.08755.x. PMID:22913516 doi:http://dx.doi.org/10.1111/j.1742-4658.2012.08755.x

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3rqr"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rqr RCSB], [http://www.ebi.ac.uk/pdbsum/3rqr PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RYR1_RABIT RYR1_RABIT]] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity).<ref>PMID:10388749</ref> <ref>PMID:22036948</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3rqr

From Proteopedia

Revision as of 15:04, 24 December 2014

Crystal structure of the RYR domain of the rabbit ryanodine receptor

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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