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1bo1
From Proteopedia
(Difference between revisions)
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<StructureSection load='1bo1' size='340' side='right'caption='[[1bo1]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1bo1' size='340' side='right'caption='[[1bo1]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1bo1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BO1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1bo1]] is a 2 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=1BO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BO1 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=1bo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bo1 OCA], [https://pdbe.org/1bo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1bo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bo1 ProSAT]</span></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=1bo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bo1 OCA], [https://pdbe.org/1bo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1bo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bo1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PI42B_HUMAN PI42B_HUMAN] Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.<ref>PMID:9038203</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1bo1 ConSurf]. | </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=1bo1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Phosphoinositide kinases play central roles in signal transduction by phosphorylating the inositol ring at specific positions. The structure of one such enzyme, type IIbeta phosphatidylinositol phosphate kinase, reveals a protein kinase ATP-binding core and demonstrates that all phosphoinositide kinases belong to one superfamily. The enzyme is a disc-shaped homodimer with a 33 x 48 A basic flat face that suggests an electrostatic mechanism for plasma membrane targeting. Conserved basic residues form a putative phosphatidylinositol phosphate specificity site. The substrate-binding site is open on one side, consistent with dual specificity for phosphatidylinositol 3- and 5-phosphates. A modeled complex with membrane-bound substrate and ATP shows how a phosphoinositide kinase can phosphorylate its substrate in situ at the membrane interface. | ||
| - | |||
| - | Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation.,Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH Cell. 1998 Sep 18;94(6):829-39. PMID:9753329<ref>PMID:9753329</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1bo1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Anderson | + | [[Category: Anderson RA]] |
| - | [[Category: Boronenkov | + | [[Category: Boronenkov IV]] |
| - | [[Category: Hurley | + | [[Category: Hurley JH]] |
| - | [[Category: Misra | + | [[Category: Misra S]] |
| - | [[Category: Rao | + | [[Category: Rao VD]] |
| - | + | ||
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Current revision
PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA
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