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4cml
From Proteopedia
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| - | + | ==Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate== | |
| - | + | <StructureSection load='4cml' size='340' side='right' caption='[[4cml]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4cml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CML FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=52N:1,2-DIOCTANOYL+PHOSPHATIDYL+EPI-INOSITOL+(3,4)-BISPHOSPHATE'>52N</scene>, <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=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cmn|4cmn]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoinositide_5-phosphatase Phosphoinositide 5-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.36 3.1.3.36] </span></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=4cml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cml OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cml RCSB], [http://www.ebi.ac.uk/pdbsum/4cml PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Phosphoinositide 5-phosphatase]] | [[Category: Phosphoinositide 5-phosphatase]] | ||
[[Category: Arrowsmith, C H.]] | [[Category: Arrowsmith, C H.]] | ||
Revision as of 07:03, 21 May 2014
Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate
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Categories: Human | Phosphoinositide 5-phosphatase | Arrowsmith, C H. | Berglund, H. | Bountra, C. | Edwards, A M. | Ekblad, T. | Flodin, S. | Graslund, S. | Karlberg, T. | Moche, M. | Nordlund, P. | Nyman, T. | Schuler, H. | Silvander, C. | Thorsell, A G. | Tresaugues, L. | Weigelt, J. | Welin, M. | Hydrolase | Magnesium binding | Sgc | Signalling | Structural genomics consortium stockholm
