3hsm
From Proteopedia
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{{STRUCTURE_3hsm| PDB=3hsm | SCENE= }} | {{STRUCTURE_3hsm| PDB=3hsm | SCENE= }} | ||
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===Crystal structure of distal N-terminal beta-trefoil domain of Ryanodine Receptor type 1=== | ===Crystal structure of distal N-terminal beta-trefoil domain of Ryanodine Receptor type 1=== | ||
+ | {{ABSTRACT_PUBMED_19541610}} | ||
- | + | ==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> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:019541610</ref><references group="xtra"/> | + | <ref group="xtra">PMID:019541610</ref><references group="xtra"/><references/> |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Amador, F J.]] | [[Category: Amador, F J.]] | ||
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[[Category: Wilson, A.]] | [[Category: Wilson, A.]] | ||
[[Category: Beta-trefoil]] | [[Category: Beta-trefoil]] | ||
- | [[Category: Calcium]] | ||
[[Category: Calcium channel]] | [[Category: Calcium channel]] | ||
[[Category: Calcium transport]] | [[Category: Calcium transport]] |
Revision as of 09:26, 27 March 2013
Contents |
Crystal structure of distal N-terminal beta-trefoil domain of Ryanodine Receptor type 1
Template:ABSTRACT PUBMED 19541610
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]
About this Structure
3hsm is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
- Amador FJ, Liu S, Ishiyama N, Plevin MJ, Wilson A, MacLennan DH, Ikura M. Crystal structure of type I ryanodine receptor amino-terminal beta-trefoil domain reveals a disease-associated mutation "hot spot" loop. Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11040-4. Epub 2009 Jun 18. PMID:19541610
- ↑ 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
Categories: Oryctolagus cuniculus | Amador, F J. | Ikura, M. | Ishiyama, N. | Liu, S. | MacLennan, D H. | Plevin, M J. | Wilson, A. | Beta-trefoil | Calcium channel | Calcium transport | Glycoprotein | Ion transport | Ionic channel | Membrane | Phosphoprotein | Receptor | S-nitrosylation | Signaling protein | Transmembrane | Transport