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Ryanodine receptor: Difference between revisions

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<StructureSection load='2xoa' size='340' side='right' caption='Rabbit ryanodine receptor 1 N-terminal (PDB code [[2xoa]])' scene=''>
<StructureSection load='2xoa' size='340' side='right' caption='Rabbit ryanodine receptor 1 N-terminal (PDB code [[2xoa]])' scene=''>
__TOC__
== Function ==
== Function ==
'''Ryanodine receptors''' (RyR) are the largest (over 5000 residues) ion channels and are responsible for the release of Ca+2 ions from the sarco/endoplasmic reticulum<ref>PMID:12270947</ref>.  RyR is a homotetramer which opens upon binding of Ca+2.  RyR is modulated by various ions, small molecules and proteins.  The protein modulators include calmodulin, FKBP, protein phosphatase and protein kinase A.  The C-terminal of RyR forms the transmembrane ion-conducting pore.  The N-terminal of RyR named “foot”, includes a trefoil knot fold and interacts with the various modulators.  The corners of the RYR cytoplasmic area are called “clamp” and undergo conformational change upon opening or closing of the channel.  RYR domains include three SPRY domains.  SPRY2 forms the link between the N terminal gating ring and the clamp region.  RYR1 and RYR2 have several phosphorylation sites.  Ryanodine is a plant alkaloid which binds to RyR with high affinity and locks the channel in an open state. There are 3 RyR isoforms.<br />
'''Ryanodine receptors''' (RyR) are the largest (over 5000 residues) ion channels and are responsible for the release of Ca+2 ions from the sarco/endoplasmic reticulum<ref>PMID:12270947</ref>.  RyR is a homotetramer which opens upon binding of Ca+2.  RyR is modulated by various ions, small molecules and proteins.  The protein modulators include calmodulin, FKBP, protein phosphatase and protein kinase A.  The C-terminal of RyR forms the transmembrane ion-conducting pore.  The N-terminal of RyR named “foot”, includes a trefoil knot fold and interacts with the various modulators.  The corners of the RYR cytoplasmic area are called “clamp” and undergo conformational change upon opening or closing of the channel.  RYR domains include three SPRY domains.  SPRY2 forms the link between the N terminal gating ring and the clamp region.  RYR1 and RYR2 have several phosphorylation sites.  Ryanodine is a plant alkaloid which binds to RyR with high affinity and locks the channel in an open state. There are 3 RyR isoforms.<br />
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== Disease ==
== Disease ==
Mutations in RyR are associated with skeletal muscle disorders and triggered cardiac arrhythmia<ref>PMID:23459219</ref><ref>PMID:10790202</ref>.  The N-terminal of RYR was found to be the disease hot spot of the molecule<ref>PMID:21048710</ref>.
Mutations in RyR are associated with skeletal muscle disorders and triggered cardiac arrhythmia<ref>PMID:23459219</ref><ref>PMID:10790202</ref>.  The N-terminal of RYR was found to be the disease hot spot of the molecule<ref>PMID:21048710</ref>.
</StructureSection>


== 3D Structures of ryanodine receptor ==
== 3D Structures of ryanodine receptor ==
[[Ryanodine receptor 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Ryanodine receptor 1
 
**[[3hsm]], [[3ila]] – rRyR1 N terminal b-trefoil domain residues 1-210 – rabbit <br />
**[[2xoa]] – rRyR1 N terminal residues 1-559<br />
**[[4i0y]], [[4i1e]], [[4i2s]], [[4i37]], [[4i3n]], [[4i6i]], [[4i8m]] – rRyR1 N terminal residues 1-559 (mutant)<br />
**[[4i96]] – rRyR1 N terminal residues 217-536 <br />
**[[5c33]] – rRyR1 SPRY1 domain residues 650-844 <br />
**[[5c30]] – rRyR1 repeat 12 domain residues 857-1054 <br />
**[[4p9j]] – rRyR1 SPRY2 domain residues 1070-1246 <br />
**[[3rqr]] – rRyR1 phosphorylation domain residues 2733-2940 + tetrapeptide<br />
**[[4ert]] – rRyR1 phosphorylation domain residues 2733-2940 <br />
**[[4esu]], [[4ett]], [[4etu]] – rRyR1 phosphorylation domain residues 2733-2940 (mutant)<br />
**[[4uwa]], [[4uwe]], [[5j8v]] – rRyR1 – Cryo EM <br />
**[[5tb0]], [[5taw]], [[5tax]], [[5tay]], [[5taz]], [[5t15]], [[5t9m]], [[5t9n]], [[5t9r]], [[5t9s]], [[5t9v]], [[5tb0]], [[5tb1]], [[5tb2]], [[5tb3]], [[5tb4]], [[5gky]], [[5gkz]], [[5gl0]], [[5gl1]] – rRyR1 + FKBP1B – Cryo EM <br />
**[[5ta3]], [[5tal]], [[5tam]], [[5tan]], [[5tap]], [[5taq]], [[5tas]], [[5tat]], [[5tau]], [[5tav]] – rRyR1 + FKBP1B + caffeine + ATP – Cryo EM <br />
**[[6fg3]] – rRyR1 + ryanodine + ATP – Cryo EM <br />
**[[6foo]] – rRyR1 + ATP – Cryo EM <br />
**[[3j8h]] – rRyR1 + FKBP12 – Cryo EM <br />
**[[5y9v]] – RyR1 N terminal - diamondback moth <br />
 
*Ryanodine receptor 2 (Cardiac Ca+2 release channel); domains - N terminal 1-547; SPRY2 1080-1253; phosphorylation 2699-2904
 
**[[3im5]] – mRyR2 N terminal – mouse <br />
**[[3im6]], [[3im7]], [[4kei]], [[4kej]], [[4kek]] – mRyR2 N terminal (mutant) <br />
**[[2mc2]] – mRyR2 N terminal - NMR <br />
**[[3qr5]] – mRyR2 N terminal <br />
**[[4etv]] – mRyR2 phosphorylation domain (mutant) <br />
**[[4l4h]] – mRyR2 N terminal <br />
**[[4l4i]] – mRyR2 N terminal (mutant) <br />
**[[4p9i]] – mRyR2 SPRY2 domain <br />
**[[4p9l]], [[5vsn]] – mRyR2 SPRY2 domain (mutant)<br />
**[[4jkq]] – hRyR2 N terminal - human <br />
**[[5go9]], [[5goa]] – RyR2 – pig - Cryo EM <br />
**[[5l1d]] – rRyR2 + FKBP12 – Cryo EM <br />
 
*Ryanodine receptor 3


**[[4erv]] – hRyR3 residues 2597-2800  <br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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Michal Harel
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