3qr5
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 3: | Line 3: | ||
<StructureSection load='3qr5' size='340' side='right'caption='[[3qr5]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3qr5' size='340' side='right'caption='[[3qr5]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3qr5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3qr5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QR5 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=3qr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr5 OCA], [https://pdbe.org/3qr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr5 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr5 ProSAT]</span></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=3qr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr5 OCA], [https://pdbe.org/3qr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr5 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RYR2_MOUSE RYR2_MOUSE] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development.<ref>PMID:10473538</ref> <ref>PMID:9628868</ref> <ref>PMID:21098440</ref> <ref>PMID:20431056</ref> | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mutations in the cardiac Ryanodine Receptor (RYR2) are linked to triggered arrhythmias. Removal of exon 3 results in a severe form of catecholaminergic polymorphic ventricular tachycardia (CPVT). This exon encodes secondary structure elements that are crucial for folding of the N-terminal domain (NTD), raising the question of why the deletion is neither lethal nor confers a loss of function. We determined the 2.3 A crystal structure of the NTD lacking exon 3. The removal causes a structural rescue whereby a flexible loop inserts itself into the beta trefoil domain and increases thermal stability. The exon 3 deletion is not tolerated in the corresponding RYR1 domain. The rescue shows a novel mechanism by which RYR2 channels can adjust their Ca(2)(+) release properties through altering the structure of the NTD. Despite the rescue, the deletion affects interfaces with other RYR2 domains. We propose that relative movement of the NTD is allosterically coupled to the pore region. | ||
| + | |||
| + | The deletion of exon 3 in the cardiac ryanodine receptor is rescued by beta strand switching.,Lobo PA, Kimlicka L, Tung CC, Van Petegem F Structure. 2011 Jun 8;19(6):790-8. doi: 10.1016/j.str.2011.03.016. PMID:21645850<ref>PMID:21645850</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3qr5" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 18: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Lobo | + | [[Category: Lobo PA]] |
| - | [[Category: Petegem | + | [[Category: Van Petegem F]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Structure of the first domain of a cardiac Ryanodine Receptor mutant with exon 3 deleted
| |||||||||||
