1fgz: Difference between revisions

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[[Image:1fgz.jpg|left|200px]]
{{Seed}}
[[Image:1fgz.png|left|200px]]


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{{STRUCTURE_1fgz|  PDB=1fgz  |  SCENE=  }}  
{{STRUCTURE_1fgz|  PDB=1fgz  |  SCENE=  }}  


'''GRP1 PH DOMAIN (UNLIGANDED)'''
===GRP1 PH DOMAIN (UNLIGANDED)===




==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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{{ABSTRACT_PUBMED_10983985}}


==About this Structure==
==About this Structure==
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[[Category: Lietzke, S E.]]
[[Category: Lietzke, S E.]]
[[Category: Ph domain]]
[[Category: Ph domain]]
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