1bo1

<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BO1 FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1-phosphatidylinositol-4-phosphate_5-kinase 1-phosphatidylinositol-4-phosphate 5-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.68 2.7.1.68] </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=1bo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bo1 OCA], [http://pdbe.org/1bo1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bo1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bo1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bo1 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PI42B_HUMAN PI42B_HUMAN]] Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.<ref>PMID:9038203</ref>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1bo1" style="background-color:#fffaf0;"></div>

[[Category: 1-phosphatidylinositol-4-phosphate 5-kinase]]

[[Category: Anderson, R A]]

[[Category: Boronenkov, I V]]

[[Category: Hurley, J H]]

[[Category: Misra, S]]

[[Category: Rao, V D]]

[[Category: Transferase]]