1bo1

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Anderson, R.A.]]
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[[Category: Anderson, R A.]]
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[[Category: Boronenkov, I.V.]]
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[[Category: Boronenkov, I V.]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
[[Category: Misra, S.]]
[[Category: Misra, S.]]
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[[Category: Rao, V.D.]]
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[[Category: Rao, V D.]]
[[Category: lipid signaling]]
[[Category: lipid signaling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:33:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:17 2008''

Revision as of 09:57, 21 February 2008


1bo1, resolution 3.0Å

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PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA

Overview

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.

About this Structure

1BO1 is a Single protein structure of sequence from Homo sapiens. Active as 1-phosphatidylinositol-4-phosphate 5-kinase, with EC number 2.7.1.68 Full crystallographic information is available from OCA.

Reference

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

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