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1n4k

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Revision as of 08:23, 24 December 2014

Crystal 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.
Ligands:
Gene:	ITPR1 OR INSP3R (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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 PubMed

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.

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.

References

↑ 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
↑ 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
↑ 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
↑ 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. Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand. Nature. 2002 Dec 12;420(6916):696-700. Epub 2002 Nov 17. PMID:12442173 doi:10.1038/nature01268

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n4k"

@@ Line 3: / Line 3: @@
 == 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>
-</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><br>
+</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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 </StructureSection>
 [[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: B-trefoil fold]]

1n4k

From Proteopedia

Revision as of 08:23, 24 December 2014

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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