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New page: left|200px<br /> <applet load="1fao" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fao, resolution 1.80Å" /> '''STRUCTURE OF THE PL...
 
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[[Image:1fao.gif|left|200px]]<br />
[[Image:1fao.gif|left|200px]]<br /><applet load="1fao" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1fao" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1fao, resolution 1.80&Aring;" />
caption="1fao, resolution 1.80&Aring;" />
'''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH IN COMPLEX WITH INOSITOL 1,3,4,5-TETRAKISPHOSPHATE'''<br />
'''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH IN COMPLEX WITH INOSITOL 1,3,4,5-TETRAKISPHOSPHATE'''<br />


==Overview==
==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.
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.


==About this Structure==
==About this Structure==
1FAO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with 4IP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAO OCA].  
1FAO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=4IP:'>4IP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAO OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ferguson, K.M.]]
[[Category: Ferguson, K M.]]
[[Category: Fournier, E.]]
[[Category: Fournier, E.]]
[[Category: Isakoff, S.J.]]
[[Category: Isakoff, S J.]]
[[Category: Kavran, J.M.]]
[[Category: Kavran, J M.]]
[[Category: Lemmon, M.A.]]
[[Category: Lemmon, M A.]]
[[Category: Sankaran, V.G.]]
[[Category: Sankaran, V G.]]
[[Category: Skolnik, E.Y.]]
[[Category: Skolnik, E Y.]]
[[Category: 4IP]]
[[Category: 4IP]]
[[Category: 3-phosphoinositides]]
[[Category: 3-phosphoinositides]]
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[[Category: pleckstrin]]
[[Category: pleckstrin]]


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