This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fgz
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1fgz.jpg|left|200px]] | [[Image:1fgz.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1fgz", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1fgz| PDB=1fgz | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''GRP1 PH DOMAIN (UNLIGANDED)''' | '''GRP1 PH DOMAIN (UNLIGANDED)''' | ||
| Line 32: | Line 29: | ||
[[Category: Lambright, D G.]] | [[Category: Lambright, D G.]] | ||
[[Category: Lietzke, S E.]] | [[Category: Lietzke, S E.]] | ||
| - | [[Category: | + | [[Category: Ph domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:18:52 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:18, 2 May 2008
GRP1 PH DOMAIN (UNLIGANDED)
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
1FGZ is a Single protein structure of sequence from Mus musculus. 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 Page seeded by OCA on Fri May 2 16:18:52 2008
