1bo1

From Proteopedia

(Difference between revisions)

Revision as of 07:01, 24 February 2021

PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA

Structural highlights

1bo1 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	1-phosphatidylinositol-4-phosphate 5-kinase, with EC number 2.7.1.68
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PI42B_HUMAN] Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.^[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 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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Castellino AM, Parker GJ, Boronenkov IV, Anderson RA, Chao MV. A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase. J Biol Chem. 1997 Feb 28;272(9):5861-70. PMID:9038203
↑ Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. Cell. 1998 Sep 18;94(6):829-39. PMID:9753329

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bo1"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bo1' size='340' side='right'caption='[[1bo1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BO1 FirstGlance]. <br>
+<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>
-</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>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1-phosphatidylinositol-4-phosphate_5-kinase 1-phosphatidylinositol-4-phosphate 5-kinase], with EC number [https://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>
+<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>
 == Function ==
-[[http://www.uniprot.org/uniprot/PI42B_HUMAN PI42B_HUMAN]] Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.<ref>PMID:9038203</ref>
+[[https://www.uniprot.org/uniprot/PI42B_HUMAN PI42B_HUMAN]] Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.<ref>PMID:9038203</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1bo1

From Proteopedia

Revision as of 07:01, 24 February 2021

PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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