1n4k: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1n4k]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N4K FirstGlance]. <br> | <table><tr><td colspan='2'>[[1n4k]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N4K FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITPR1 OR INSP3R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITPR1 OR INSP3R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n4k RCSB], [http://www.ebi.ac.uk/pdbsum/1n4k PDBsum]</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=1n4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n4k RCSB], [http://www.ebi.ac.uk/pdbsum/1n4k PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Alattia, J R | [[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, T K | [[Category: Mal, T K]] | ||
[[Category: Michikawa, T | [[Category: Michikawa, T]] | ||
[[Category: Mikoshiba, K | [[Category: Mikoshiba, K]] | ||
[[Category: Talarico, S | [[Category: Talarico, S]] | ||
[[Category: Tong, F K | [[Category: Tong, F K]] | ||
[[Category: Tong, K I | [[Category: Tong, K I]] | ||
[[Category: Yoshikawa, F | [[Category: Yoshikawa, F]] | ||
[[Category: Armadillo-like fold]] | [[Category: Armadillo-like fold]] | ||
[[Category: B-trefoil fold]] | [[Category: B-trefoil fold]] | ||
Revision as of 11:23, 24 December 2014
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
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. Publication Abstract from PubMedIn 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. 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:12442173[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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