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[[Image:1n4k.jpg|left|200px]]


{{Structure
==Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3==
|PDB= 1n4k |SIZE=350|CAPTION= <scene name='initialview01'>1n4k</scene>, resolution 2.20&Aring;
<StructureSection load='1n4k' size='340' side='right'caption='[[1n4k]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>
<table><tr><td colspan='2'>[[1n4k]] is a 1 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=1N4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4K FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE= ITPR1 OR INSP3R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></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=1n4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4k OCA], [https://pdbe.org/1n4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4k RCSB], [https://www.ebi.ac.uk/pdbsum/1n4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ITPR1_MOUSE ITPR1_MOUSE] 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.<ref>PMID:2554142</ref> <ref>PMID:19752026</ref> <ref>PMID:20813840</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n4/1n4k_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n4k ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3'''
==See Also==
 
*[[Inositol 1%2C4%2C5-Trisphosphate Receptor|Inositol 1%2C4%2C5-Trisphosphate Receptor]]
 
== References ==
==Overview==
<references/>
In a variety of cells, the Ca2+ signalling process is mediated by the endoplasmic-reticulum-membrane-associated Ca2+ release channel, inositol 1,4,5-trisphosphate (InsP3) receptor (InsP3R). Being ubiquitous and present in organisms ranging from humans to Caenorhabditis elegans, InsP3R has a vital role in the control of cellular and physiological processes as diverse as cell division, cell proliferation, apoptosis, fertilization, development, behaviour, memory and learning. Mouse type I InsP3R (InsP3R1), found in high abundance in cerebellar Purkinje cells, is a polypeptide with three major functionally distinct regions: the amino-terminal InsP3-binding region, the central modulatory region and the carboxy-terminal channel region. Here we present a 2.2-A crystal structure of the InsP3-binding core of mouse InsP3R1 in complex with InsP3. The asymmetric, boomerang-like structure consists of an N-terminal beta-trefoil domain and a C-terminal alpha-helical domain containing an 'armadillo repeat'-like fold. The cleft formed by the two domains exposes a cluster of arginine and lysine residues that coordinate the three phosphoryl groups of InsP3. Putative Ca2+-binding sites are identified in two separate locations within the InsP3-binding core.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1N4K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4K OCA].
 
==Reference==
Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand., Bosanac I, Alattia JR, Mal TK, Chan J, Talarico S, Tong FK, Tong KI, Yoshikawa F, Furuichi T, Iwai M, Michikawa T, Mikoshiba K, Ikura M, Nature. 2002 Dec 12;420(6916):696-700. Epub 2002 Nov 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12442173 12442173]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Alattia JR]]
[[Category: Alattia, J R.]]
[[Category: Bosanac I]]
[[Category: Bosanac, I.]]
[[Category: Chan J]]
[[Category: Chan, J.]]
[[Category: Furuichi T]]
[[Category: Furuichi, T.]]
[[Category: Ikura M]]
[[Category: Ikura, M.]]
[[Category: Iwai M]]
[[Category: Iwai, M.]]
[[Category: Mal TK]]
[[Category: Mal, T K.]]
[[Category: Michikawa T]]
[[Category: Michikawa, T.]]
[[Category: Mikoshiba K]]
[[Category: Mikoshiba, K.]]
[[Category: Talarico S]]
[[Category: Talarico, S.]]
[[Category: Tong FK]]
[[Category: Tong, F K.]]
[[Category: Tong KI]]
[[Category: Tong, K I.]]
[[Category: Yoshikawa F]]
[[Category: Yoshikawa, F.]]
[[Category: I3P]]
[[Category: armadillo-like fold]]
[[Category: b-trefoil fold]]
[[Category: calcium channel]]
[[Category: ip3 receptor]]
[[Category: ip3-binding core]]
[[Category: protein-ligand complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:03 2008''

Latest revision as of 10:52, 14 February 2024

Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3

Structural highlights

1n4k is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ITPR1_MOUSE 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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Furuichi T, Yoshikawa S, Miyawaki A, Wada K, Maeda N, Mikoshiba K. Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400. Nature. 1989 Nov 2;342(6245):32-8. PMID:2554142 doi:http://dx.doi.org/10.1038/342032a0
  2. ↑ Li G, Mongillo M, Chin KT, Harding H, Ron D, Marks AR, Tabas I. Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol. 2009 Sep 21;186(6):783-92. doi: 10.1083/jcb.200904060. Epub 2009 Sep, 14. PMID:19752026 doi:http://dx.doi.org/10.1083/jcb.200904060
  3. ↑ Yamazaki H, Chan J, Ikura M, Michikawa T, Mikoshiba K. Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening. J Biol Chem. 2010 Nov 12;285(46):36081-91. doi: 10.1074/jbc.M110.140129. Epub, 2010 Sep 2. PMID:20813840 doi:http://dx.doi.org/10.1074/jbc.M110.140129

1n4k, resolution 2.20Å

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