1fb8

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(New page: 200px<br /> <applet load="1fb8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fb8, resolution 2.40&Aring;" /> '''STRUCTURE OF THE PL...)
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<applet load="1fb8" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1fb8, resolution 2.40&Aring;" />
'''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH'''<br />
'''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1FB8 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FB8 OCA].
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1FB8 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB8 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ferguson, K.M.]]
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[[Category: Ferguson, K M.]]
[[Category: Fournier, E.]]
[[Category: Fournier, E.]]
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[[Category: Isakoff, S.J.]]
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[[Category: Isakoff, S J.]]
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[[Category: Kavran, J.M.]]
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[[Category: Kavran, J M.]]
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[[Category: Lemmon, M.A.]]
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[[Category: Lemmon, M A.]]
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[[Category: Sankaran, V.G.]]
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[[Category: Sankaran, V G.]]
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[[Category: Skolnik, E.Y.]]
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[[Category: Skolnik, E Y.]]
[[Category: PO4]]
[[Category: PO4]]
[[Category: 3-phosphoinositides]]
[[Category: 3-phosphoinositides]]
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[[Category: pleckstrin]]
[[Category: pleckstrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:51:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:56 2008''

Revision as of 10:36, 21 February 2008


1fb8, resolution 2.40Å

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STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH

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

1FB8 is a Single protein structure of sequence from Homo sapiens with as ligand. 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

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