2fju
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(New page: 200px<br /> <applet load="2fju" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fju, resolution 2.20Å" /> '''Activated Rac1 boun...)
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Revision as of 20:00, 12 November 2007
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Activated Rac1 bound to its effector phospholipase C beta 2
Contents |
Overview
Although diverse signaling cascades require the coordinated regulation of, heterotrimeric G proteins and small GTPases, these connections remain, poorly understood. We present the crystal structure of the GTPase Rac1, bound to phospholipase C-beta2 (PLC-beta2), a classic effector of, heterotrimeric G proteins. Rac1 engages the pleckstrin-homology (PH), domain of PLC-beta2 to optimize its orientation for substrate membranes., Gbetagamma also engages the PH domain to activate PLC-beta2, and these two, activation events are compatible, leading to additive stimulation of, phospholipase activity. In contrast to PLC-delta, the PH domain of, PLC-beta2 cannot bind phosphoinositides, eliminating this mode of, regulation. The structure of the Rac1-PLC-beta2 complex reveals, determinants that dictate selectivity of PLC-beta isozymes for Rac GTPases, over other Rho-family GTPases, and substitutions within PLC-beta2 abrogate, its stimulation by Rac1 but not by Gbetagamma, allowing for functional, dissection of this integral signaling node.
Disease
Known disease associated with this structure: Platelet PLC beta-2 deficiency OMIM:[604114]
About this Structure
2FJU is a Protein complex structure of sequences from Homo sapiens with MG, CA and GSP as ligands. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 Full crystallographic information is available from OCA.
Reference
Crystal structure of Rac1 bound to its effector phospholipase C-beta2., Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J, Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. PMID:17115053
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