6mu2: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6mu2 is ~~ON HOLD until Paper~~ Publication

==Structure of full-length IP3R1 channel in the Apo-state==

== Structural highlights ==

<table><tr><td colspan='2'>[[6mu2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MU2 FirstGlance]. <br>

</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=6mu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mu2 OCA], [http://pdbe.org/6mu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mu2 RCSB], [http://www.ebi.ac.uk/pdbsum/6mu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mu2 ProSAT]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/ITPR1_RAT ITPR1_RAT]] Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity).

== Publication Abstract from PubMed ==

Inositol-1,4,5-trisphosphate receptors (InsP3Rs) are cation channels that mobilize Ca(2+) from intracellular stores in response to a wide range of cellular stimuli. The paradigm of InsP3R activation is the coupled interplay between binding of InsP3 and Ca(2+) that switches the ion conduction pathway between closed and open states to enable the passage of Ca(2+) through the channel. However, the molecular mechanism of how the receptor senses and decodes ligand-binding signals into gating motion remains unknown. Here, we present the electron cryo-microscopy structure of InsP3R1 from rat cerebellum determined to 4.1 A resolution in the presence of activating concentrations of Ca(2+) and adenophostin A (AdA), a structural mimetic of InsP3 and the most potent known agonist of the channel. Comparison with the 3.9 A-resolution structure of InsP3R1 in the Apo-state, also reported herein, reveals the binding arrangement of AdA in the tetrameric channel assembly and striking ligand-induced conformational rearrangements within cytoplasmic domains coupled to the dilation of a hydrophobic constriction at the gate. Together, our results provide critical insights into the mechanistic principles by which ligand-binding allosterically gates InsP3R channel.

~~Authors: Serysheva, I.I~~., Fan, G., Baker~~, M.R.~~, Wang, Z., Seryshev, A., ~~Ludtke~~, S.J., ~~Baker, M~~.L.

Cryo-EM reveals ligand induced allostery underlying InsP3R channel gating.,Fan G, Baker MR, Wang Z, Seryshev AB, Ludtke SJ, Baker ML, Serysheva II Cell Res. 2018 Nov 23. pii: 10.1038/s41422-018-0108-5. doi:, 10.1038/s41422-018-0108-5. PMID:30470765<ref>PMID:30470765</ref>

~~Description: Structure~~ of ~~full~~-~~length IP3R1 channel in the Apo~~-~~state~~

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

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Rattus norvegicus]]

[[Category: Baker, M L]]

[[Category: Baker, M R]]

[[Category: Fan, G]]

[[Category: Ludtke, S J]]

[[Category: Seryshev, A]]

~~[[Category: Baker, M.R]]~~

[[Category: Serysheva, I I]]

~~[[Category: Baker, M.L]]~~

~~[[Category: Fan, G]]~~

~~[[Category: Ludtke, S.J]]~~

[[Category: Serysheva, I.I]]

[[Category: Wang, Z]]

[[Category: 5-trisphosphate receptor]]

[[Category: Calcium release channel]]

[[Category: Inositol 1]]

[[Category: Membrane protein]]

[[Category: Neuronal type 1]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6mu2 is ON HOLD  until Paper Publication
+==Structure of full-length IP3R1 channel in the Apo-state==
+<StructureSection load='6mu2' size='340' side='right' caption='[[6mu2]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6mu2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MU2 FirstGlance]. <br>
+</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=6mu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mu2 OCA], [http://pdbe.org/6mu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mu2 RCSB], [http://www.ebi.ac.uk/pdbsum/6mu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mu2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ITPR1_RAT ITPR1_RAT]] Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Inositol-1,4,5-trisphosphate receptors (InsP3Rs) are cation channels that mobilize Ca(2+) from intracellular stores in response to a wide range of cellular stimuli. The paradigm of InsP3R activation is the coupled interplay between binding of InsP3 and Ca(2+) that switches the ion conduction pathway between closed and open states to enable the passage of Ca(2+) through the channel. However, the molecular mechanism of how the receptor senses and decodes ligand-binding signals into gating motion remains unknown. Here, we present the electron cryo-microscopy structure of InsP3R1 from rat cerebellum determined to 4.1 A resolution in the presence of activating concentrations of Ca(2+) and adenophostin A (AdA), a structural mimetic of InsP3 and the most potent known agonist of the channel. Comparison with the 3.9 A-resolution structure of InsP3R1 in the Apo-state, also reported herein, reveals the binding arrangement of AdA in the tetrameric channel assembly and striking ligand-induced conformational rearrangements within cytoplasmic domains coupled to the dilation of a hydrophobic constriction at the gate. Together, our results provide critical insights into the mechanistic principles by which ligand-binding allosterically gates InsP3R channel.
-Authors: Serysheva, I.I., Fan, G., Baker, M.R., Wang, Z., Seryshev, A., Ludtke, S.J., Baker, M.L.
+Cryo-EM reveals ligand induced allostery underlying InsP3R channel gating.,Fan G, Baker MR, Wang Z, Seryshev AB, Ludtke SJ, Baker ML, Serysheva II Cell Res. 2018 Nov 23. pii: 10.1038/s41422-018-0108-5. doi:, 10.1038/s41422-018-0108-5. PMID:30470765<ref>PMID:30470765</ref>
-Description: Structure of full-length IP3R1 channel in the Apo-state
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6mu2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Rattus norvegicus]]
+[[Category: Baker, M L]]
+[[Category: Baker, M R]]
+[[Category: Fan, G]]
+[[Category: Ludtke, S J]]
 [[Category: Seryshev, A]]
-[[Category: Baker, M.R]]
+[[Category: Serysheva, I I]]
-[[Category: Baker, M.L]]
-[[Category: Fan, G]]
-[[Category: Ludtke, S.J]]
-[[Category: Serysheva, I.I]]
 [[Category: Wang, Z]]
+[[Category: 5-trisphosphate receptor]]
+[[Category: Calcium release channel]]
+[[Category: Inositol 1]]
+[[Category: Membrane protein]]
+[[Category: Neuronal type 1]]