1fhx
From Proteopedia
(New page: 200px<br /><applet load="1fhx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fhx, resolution 2.50Å" /> '''Structure of the ple...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1fhx.gif|left|200px]]<br /><applet load="1fhx" size=" | + | [[Image:1fhx.gif|left|200px]]<br /><applet load="1fhx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fhx, resolution 2.50Å" /> | caption="1fhx, resolution 2.50Å" /> | ||
'''Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate'''<br /> | '''Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pleckstrin homology (PH) domains are protein modules of around 120 amino | + | 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== | ||
| - | 1FHX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 and 4IP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FHX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=4IP:'>4IP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHX OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ferguson, K | + | [[Category: Ferguson, K M.]] |
[[Category: Fournier, E.]] | [[Category: Fournier, E.]] | ||
| - | [[Category: Isakoff, S | + | [[Category: Isakoff, S J.]] |
| - | [[Category: Kavran, J | + | [[Category: Kavran, J M.]] |
| - | [[Category: Lemmon, M | + | [[Category: Lemmon, M A.]] |
| - | [[Category: Sankaran, V | + | [[Category: Sankaran, V G.]] |
| - | [[Category: Skolnik, E | + | [[Category: Skolnik, E Y.]] |
[[Category: 4IP]] | [[Category: 4IP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 27: | Line 27: | ||
[[Category: pleckstrin]] | [[Category: pleckstrin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:53 2008'' |
Revision as of 10:38, 21 February 2008
|
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.
About this Structure
1FHX is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains., Ferguson KM, Kavran JM, Sankaran VG, Fournier E, Isakoff SJ, Skolnik EY, Lemmon MA, Mol Cell. 2000 Aug;6(2):373-84. PMID:10983984
Page seeded by OCA on Thu Feb 21 12:38:53 2008
