3mtc: Difference between revisions
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New page: '''Unreleased structure''' The entry 3mtc is ON HOLD Authors: Tresaugues, L., Welin, M., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Edwards, A.M., Flodin, S., Flores, A.,... |
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The | ==Crystal Structure of INPP5B in complex with phosphatidylinositol 4-phosphate== | ||
<StructureSection load='3mtc' size='340' side='right'caption='[[3mtc]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mtc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MTC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PIF:(2R)-3-{[(S)-HYDROXY{[(1R,2R,3R,4R,5S,6R)-2,3,5,6-TETRAHYDROXY-4-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL]OXY}PROPANE-1,2-DIYL+DIOCTANOATE'>PIF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3mtc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtc OCA], [https://pdbe.org/3mtc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mtc RCSB], [https://www.ebi.ac.uk/pdbsum/3mtc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/I5P2_HUMAN I5P2_HUMAN] Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.<ref>PMID:7721860</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/mt/3mtc_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=3mtc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase subfamilies involved in insulin regulation and Lowes syndrome. The structural basis for membrane recognition, substrate specificity, and regulation of inositol polyphosphate 5-phophatases is still poorly understood. We determined the crystal structures of human SHIP2, OCRL, and INPP5B, the latter in complex with phosphoinositide substrate analogs, which revealed a membrane interaction patch likely to assist in sequestering substrates from the lipid bilayer. Residues recognizing the 1-phosphate of the substrates are highly conserved among human family members, suggesting similar substrate binding modes. However, 3- and 4-phosphate recognition varies and determines individual substrate specificity profiles. The high conservation of the environment of the scissile 5-phosphate suggests a common reaction geometry for all members of the human 5-phosphatase family. | |||
Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases.,Tresaugues L, Silvander C, Flodin S, Welin M, Nyman T, Graslund S, Hammarstrom M, Berglund H, Nordlund P Structure. 2014 Apr 2. pii: S0969-2126(14)00073-2. doi:, 10.1016/j.str.2014.01.013. PMID:24704254<ref>PMID:24704254</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3mtc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphoinositide phosphatase|Phosphoinositide phosphatase]] | |||
*[[3D structures of inositol polyphosphate 5-phosphatase OCRL|3D structures of inositol polyphosphate 5-phosphatase OCRL]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith CH]] | |||
[[Category: Berglund H]] | |||
[[Category: Bountra C]] | |||
[[Category: Collins R]] | |||
[[Category: Edwards AM]] | |||
[[Category: Flodin S]] | |||
[[Category: Flores A]] | |||
[[Category: Graslund S]] | |||
[[Category: Hammarstrom M]] | |||
[[Category: Johansson I]] | |||
[[Category: Karlberg T]] | |||
[[Category: Kol S]] | |||
[[Category: Kotenyova T]] | |||
[[Category: Moche M]] | |||
[[Category: Nordlund P]] | |||
[[Category: Nyman T]] | |||
[[Category: Persson C]] | |||
[[Category: Schuler H]] | |||
[[Category: Schutz P]] | |||
[[Category: Siponen MI]] | |||
[[Category: Thorsell AG]] | |||
[[Category: Tresaugues L]] | |||
[[Category: Wahlberg E]] | |||
[[Category: Weigelt J]] | |||
[[Category: Welin M]] | |||
[[Category: Wisniewska M]] | |||
[[Category: Van der Berg S]] | |||
Latest revision as of 12:01, 6 September 2023
Crystal Structure of INPP5B in complex with phosphatidylinositol 4-phosphateCrystal Structure of INPP5B in complex with phosphatidylinositol 4-phosphate
Structural highlights
FunctionI5P2_HUMAN Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.[1] 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 PubMedSHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase subfamilies involved in insulin regulation and Lowes syndrome. The structural basis for membrane recognition, substrate specificity, and regulation of inositol polyphosphate 5-phophatases is still poorly understood. We determined the crystal structures of human SHIP2, OCRL, and INPP5B, the latter in complex with phosphoinositide substrate analogs, which revealed a membrane interaction patch likely to assist in sequestering substrates from the lipid bilayer. Residues recognizing the 1-phosphate of the substrates are highly conserved among human family members, suggesting similar substrate binding modes. However, 3- and 4-phosphate recognition varies and determines individual substrate specificity profiles. The high conservation of the environment of the scissile 5-phosphate suggests a common reaction geometry for all members of the human 5-phosphatase family. Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases.,Tresaugues L, Silvander C, Flodin S, Welin M, Nyman T, Graslund S, Hammarstrom M, Berglund H, Nordlund P Structure. 2014 Apr 2. pii: S0969-2126(14)00073-2. doi:, 10.1016/j.str.2014.01.013. PMID:24704254[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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