1fgz: Difference between revisions

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New page: left|200px<br /><applet load="1fgz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fgz, resolution 2.05Å" /> '''GRP1 PH DOMAIN (UNLI...
 
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[[Image:1fgz.jpg|left|200px]]<br /><applet load="1fgz" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fgz.jpg|left|200px]]<br /><applet load="1fgz" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fgz, resolution 2.05&Aring;" />
caption="1fgz, resolution 2.05&Aring;" />
'''GRP1 PH DOMAIN (UNLIGANDED)'''<br />
'''GRP1 PH DOMAIN (UNLIGANDED)'''<br />


==Overview==
==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.
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==
1FGZ 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FGZ OCA].  
1FGZ 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGZ OCA].  


==Reference==
==Reference==
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[[Category: Chawla, A.]]
[[Category: Chawla, A.]]
[[Category: Cronin, T.]]
[[Category: Cronin, T.]]
[[Category: Czech, M.P.]]
[[Category: Czech, M P.]]
[[Category: Klarlund, J.]]
[[Category: Klarlund, J.]]
[[Category: Lambright, D.G.]]
[[Category: Lambright, D G.]]
[[Category: Lietzke, S.E.]]
[[Category: Lietzke, S E.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: ph domain]]
[[Category: ph domain]]


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