1fhw: Difference between revisions
New page: left|200px<br /><applet load="1fhw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fhw, resolution 1.90Å" /> '''Structure of the ple... |
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[[Image:1fhw.gif|left|200px]]<br /><applet load="1fhw" size=" | [[Image:1fhw.gif|left|200px]]<br /><applet load="1fhw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fhw, resolution 1.90Å" /> | caption="1fhw, resolution 1.90Å" /> | ||
'''Structure of the pleckstrin homology domain from GRP1 in complex with inositol(1,3,4,5,6)pentakisphosphate'''<br /> | '''Structure of the pleckstrin homology domain from GRP1 in complex with inositol(1,3,4,5,6)pentakisphosphate'''<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== | ||
1FHW 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 I5P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1FHW 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=I5P:'>I5P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHW OCA]. | ||
==Reference== | ==Reference== | ||
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[[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: I5P]] | [[Category: I5P]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: pleckstrin]] | [[Category: pleckstrin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:51 2008'' | ||
Revision as of 13:38, 21 February 2008
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Structure of the pleckstrin homology domain from GRP1 in complex with inositol(1,3,4,5,6)pentakisphosphate
OverviewOverview
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 StructureAbout this Structure
1FHW is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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