4uwe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:24, 9 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Structure of the ryanodine receptor at resolution of 8.5 A in partially open state==
==Structure of the ryanodine receptor at resolution of 8.5 A in partially open state==
-
<StructureSection load='4uwe' size='340' side='right' caption='[[4uwe]], [[Resolution|resolution]] 8.50&Aring;' scene=''>
+
<SX load='4uwe' size='340' side='right' viewer='molstar' caption='[[4uwe]], [[Resolution|resolution]] 8.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4uwe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UWE FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4uwe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UWE FirstGlance]. <br>
-
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.5&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uwa|4uwa]]</td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uwe OCA], [https://pdbe.org/4uwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uwe RCSB], [https://www.ebi.ac.uk/pdbsum/4uwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uwe ProSAT]</span></td></tr>
-
<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=4uwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uwe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uwe RCSB], [http://www.ebi.ac.uk/pdbsum/4uwe PDBsum]</span></td></tr>
+
</table>
</table>
 +
== Function ==
 +
[https://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 ==
 +
Muscle contraction is initiated by the release of calcium (Ca2+) from the sarcoplasmic reticulum into the cytoplasm of myocytes through ryanodine receptors (RyRs). RyRs are homotetrameric channels with a molecular mass of more than 2.2 megadaltons that are regulated by several factors, including ions, small molecules and proteins. Numerous mutations in RyRs have been associated with human diseases. The molecular mechanism underlying the complex regulation of RyRs is poorly understood. Using electron cryomicroscopy, here we determine the architecture of rabbit RyR1 at a resolution of 6.1 A. We show that the cytoplasmic moiety of RyR1 contains two large alpha-solenoid domains and several smaller domains, with folds suggestive of participation in protein-protein interactions. The transmembrane domain represents a chimaera of voltage-gated sodium and pH-activated ion channels. We identify the calcium-binding EF-hand domain and show that it functions as a conformational switch allosterically gating the channel.
 +
 +
Architecture and conformational switch mechanism of the ryanodine receptor.,Efremov RG, Leitner A, Aebersold R, Raunser S Nature. 2014 Dec 1. doi: 10.1038/nature13916. PMID:25470059<ref>PMID:25470059</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4uwe" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
-
</StructureSection>
+
</SX>
 +
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Aebersold, R]]
+
[[Category: Aebersold R]]
-
[[Category: Efremov, R G]]
+
[[Category: Efremov RG]]
-
[[Category: Leitner, A]]
+
[[Category: Leitner A]]
-
[[Category: Raunser, S]]
+
[[Category: Raunser S]]
-
[[Category: Calcium binding]]
+
-
[[Category: Conformational changes]]
+
-
[[Category: Ion channel]]
+
-
[[Category: Muscular contraction]]
+
-
[[Category: Signaling protein]]
+

Current revision

Structure of the ryanodine receptor at resolution of 8.5 A in partially open state

4uwe, resolution 8.50Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools