1fgy

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(New page: 200px<br /><applet load="1fgy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fgy, resolution 1.5&Aring;" /> '''GRP1 PH DOMAIN WITH I...)
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[[Image:1fgy.jpg|left|200px]]<br /><applet load="1fgy" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fgy.jpg|left|200px]]<br /><applet load="1fgy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fgy, resolution 1.5&Aring;" />
caption="1fgy, resolution 1.5&Aring;" />
'''GRP1 PH DOMAIN WITH INS(1,3,4,5)P4'''<br />
'''GRP1 PH DOMAIN WITH INS(1,3,4,5)P4'''<br />
==Overview==
==Overview==
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Lipid second messengers generated by phosphoinositide (PI) 3-kinases, regulate diverse cellular functions through interaction with pleckstrin, homology (PH) domains in modular signaling proteins. The PH domain of, Grp1, a PI 3-kinase-activated exchange factor for Arf GTPases, selectively, binds phosphatidylinositol 3,4,5-trisphosphate with high affinity. We have, determined the structure of the Grp1 PH domain in the unliganded form and, bound to inositol 1,3,4,5-tetraphosphate. A novel mode of phosphoinositide, recognition involving a 20-residue insertion within the beta6/beta7 loop, explains the unusually high specificity of the Grp1 PH domain and the, promiscuous 3-phosphoinositide binding typical of several PH domains, including that of protein kinase B. When compared to other PH domains, general determinants of 3-phosphoinositide recognition and specificity can, be deduced.
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Lipid second messengers generated by phosphoinositide (PI) 3-kinases regulate diverse cellular functions through interaction with pleckstrin homology (PH) domains in modular signaling proteins. The PH domain of Grp1, a PI 3-kinase-activated exchange factor for Arf GTPases, selectively binds phosphatidylinositol 3,4,5-trisphosphate with high affinity. We have determined the structure of the Grp1 PH domain in the unliganded form and bound to inositol 1,3,4,5-tetraphosphate. A novel mode of phosphoinositide recognition involving a 20-residue insertion within the beta6/beta7 loop explains the unusually high specificity of the Grp1 PH domain and the promiscuous 3-phosphoinositide binding typical of several PH domains including that of protein kinase B. When compared to other PH domains, general determinants of 3-phosphoinositide recognition and specificity can be deduced.
==About this Structure==
==About this Structure==
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1FGY 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 4IP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FGY OCA].
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1FGY 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=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=1FGY OCA].
==Reference==
==Reference==
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[[Category: Chawla, A.]]
[[Category: Chawla, A.]]
[[Category: Cronin, T.]]
[[Category: Cronin, T.]]
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[[Category: Czech, M.P.]]
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[[Category: Czech, M P.]]
[[Category: Klarlund, J.]]
[[Category: Klarlund, J.]]
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[[Category: Lambright, D.G.]]
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[[Category: Lambright, D G.]]
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[[Category: Lietzke, S.E.]]
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[[Category: Lietzke, S E.]]
[[Category: 4IP]]
[[Category: 4IP]]
[[Category: ph domain]]
[[Category: ph domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:55:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:33 2008''

Revision as of 10:38, 21 February 2008

Image:1fgy.jpg

1fgy, resolution 1.5Å

Drag the structure with the mouse to rotate

GRP1 PH DOMAIN WITH INS(1,3,4,5)P4

Overview

Lipid second messengers generated by phosphoinositide (PI) 3-kinases regulate diverse cellular functions through interaction with pleckstrin homology (PH) domains in modular signaling proteins. The PH domain of Grp1, a PI 3-kinase-activated exchange factor for Arf GTPases, selectively binds phosphatidylinositol 3,4,5-trisphosphate with high affinity. We have determined the structure of the Grp1 PH domain in the unliganded form and bound to inositol 1,3,4,5-tetraphosphate. A novel mode of phosphoinositide recognition involving a 20-residue insertion within the beta6/beta7 loop explains the unusually high specificity of the Grp1 PH domain and the promiscuous 3-phosphoinositide binding typical of several PH domains including that of protein kinase B. When compared to other PH domains, general determinants of 3-phosphoinositide recognition and specificity can be deduced.

About this Structure

1FGY is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains., Lietzke SE, Bose S, Cronin T, Klarlund J, Chawla A, Czech MP, Lambright DG, Mol Cell. 2000 Aug;6(2):385-94. PMID:10983985

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