1fhx: Difference between revisions

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[[Image:1fhx.~~gif~~|left|200px]]

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

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~~'''~~Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate~~'''~~

===Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate===

~~==Overview==~~

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~~Pleckstrin homology (PH) domains are protein modules of around 120 amino acids found in many proteins involved in cellular signaling. Certain PH domains drive signal~~-~~dependent membrane recruitment of their host proteins by binding strongly and specifically to lipid second messengers produced by agonist~~-~~stimulated phosphoinositide 3-kinases (PI 3-Ks). We describe X-ray crystal structures of two different PH domains bound to Ins(1,3,4~~,~~5)P4~~, the ~~head group of~~ the ~~major PI 3-K product PtdIns~~(~~3,4,5)P3~~. ~~One of these PH domains (from Grp1~~) is ~~PtdIns(3,4,5)P3 specific, while~~ the ~~other (from DAPP1/PHISH) binds strongly to both PtdIns(3,4,5)P3 and its 5'~~-~~dephosphorylation product, PtdIns(3,4)P2. Comparison of the two structures provides an explanation for the distinct phosphoinositide specificities of the two PH domains and allows us to predict the 3~~-~~phosphoinositide selectivity of uncharacterized PH domains.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10983984}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10983984 is the PubMed ID number.

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==About this Structure==

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[[Category: Inositol tetrakisphosphate signal transduction protein]]

[[Category: Pleckstrin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 16:~~20:45~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:16:23 2008''

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-[[Image:1fhx.gif|left|200px]]
+{{Seed}}
+[[Image:1fhx.png|left|200px]]
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 {{STRUCTURE_1fhx|  PDB=1fhx  |  SCENE=  }}
-'''Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate'''
+===Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate===
-==Overview==
+<!--
-Pleckstrin homology (PH) domains are protein modules of around 120 amino acids found in many proteins involved in cellular signaling. Certain PH domains drive signal-dependent membrane recruitment of their host proteins by binding strongly and specifically to lipid second messengers produced by agonist-stimulated phosphoinositide 3-kinases (PI 3-Ks). We describe X-ray crystal structures of two different PH domains bound to Ins(1,3,4,5)P4, the head group of the major PI 3-K product PtdIns(3,4,5)P3. One of these PH domains (from Grp1) is PtdIns(3,4,5)P3 specific, while the other (from DAPP1/PHISH) binds strongly to both PtdIns(3,4,5)P3 and its 5'-dephosphorylation product, PtdIns(3,4)P2. Comparison of the two structures provides an explanation for the distinct phosphoinositide specificities of the two PH domains and allows us to predict the 3-phosphoinositide selectivity of uncharacterized PH domains.
+The line below this paragraph, {{ABSTRACT_PUBMED_10983984}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10983984 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10983984}}
 ==About this Structure==
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 [[Category: Inositol tetrakisphosphate signal transduction protein]]
 [[Category: Pleckstrin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:20:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:16:23 2008''