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4BG6

14-3-3 interaction with Rnd3 prenyl-phosphorylation motif

Summary for 4BG6
Entry DOI10.2210/pdb4bg6/pdb
Descriptor14-3-3 PROTEIN ZETA/DELTA, RHO-RELATED GTP-BINDING PROTEIN RHOE, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, ... (5 entities in total)
Functional Keywordssignaling protein, prenylation, actin cytoskeleton
Biological sourceHOMO SAPIENS (HUMAN)
More
Total number of polymer chains4
Total formula weight59524.94
Authors
Riou, P.,Kjaer, S.,Purkiss, A.,O'Reilly, N.,McDonald, N.Q. (deposition date: 2013-03-23, release date: 2013-05-29, Last modification date: 2024-11-20)
Primary citationRiou, P.,Kjaer, S.,Garg, R.,Purkiss, A.,George, R.,Cain, R.J.,Bineva, G.,Reymond, N.,Mccoll, B.,Thompson, A.J.,O'Reilly, N.,Mcdonald, N.Q.,Parker, P.J.,Ridley, A.J.
14-3-3 Proteins Interact with a Hybrid Prenyl-Phosphorylation Motif to Inhibit G Proteins.
Cell(Cambridge,Mass.), 153:640-, 2013
Cited by
PubMed Abstract: Signaling through G proteins normally involves conformational switching between GTP- and GDP-bound states. Several Rho GTPases are also regulated by RhoGDI binding and sequestering in the cytosol. Rnd proteins are atypical constitutively GTP-bound Rho proteins, whose regulation remains elusive. Here, we report a high-affinity 14-3-3-binding site at the C terminus of Rnd3 consisting of both the Cys241-farnesyl moiety and a Rho-associated coiled coil containing protein kinase (ROCK)-dependent Ser240 phosphorylation site. 14-3-3 binding to Rnd3 also involves phosphorylation of Ser218 by ROCK and/or Ser210 by protein kinase C (PKC). The crystal structure of a phosphorylated, farnesylated Rnd3 peptide with 14-3-3 reveals a hydrophobic groove in 14-3-3 proteins accommodating the farnesyl moiety. Functionally, 14-3-3 inhibits Rnd3-induced cell rounding by translocating it from the plasma membrane to the cytosol. Rnd1, Rnd2, and geranylgeranylated Rap1A interact similarly with 14-3-3. In contrast to the canonical GTP/GDP switch that regulates most Ras superfamily members, our results reveal an unprecedented mechanism for G protein inhibition by 14-3-3 proteins.
PubMed: 23622247
DOI: 10.1016/J.CELL.2013.03.044
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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