1bo1: Difference between revisions

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[[Image:1bo1.~~jpg~~|left|200px]]

[[Image:1bo1.png|left|200px]]

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~~'''~~PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA~~'''~~

===PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9753329}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9753329 is the PubMed ID number.

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==About this Structure==

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[[Category: Rao, V D.]]

[[Category: Lipid signaling]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:45:11 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:26:38 2008''

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-[[Image:1bo1.jpg|left|200px]]
+{{Seed}}
+[[Image:1bo1.png|left|200px]]
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 {{STRUCTURE_1bo1|  PDB=1bo1  |  SCENE=  }}
-'''PHOSPHATIDYLINOSITOL PHOSPHATE KINASE TYPE II BETA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9753329}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9753329 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9753329}}
 ==About this Structure==
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 [[Category: Rao, V D.]]
 [[Category: Lipid signaling]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:45:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:26:38 2008''