EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	E2 variants for probing E3 ubiquitin ligase activities.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 123, Issue 1, Page e2524899122, Year 2026
掲載日	2026年1月6日
著者	Jiale Du / Gisele A Andree / Daniel Horn-Ghetko / Luca Stier / Jaspal Singh / Sebastian Kostrhon / Leo Kiss / Matthias Mann / Sachdev S Sidhu / Brenda A Schulman /
PubMed 要旨	E3 ligases partner with E2 enzymes to regulate vast eukaryotic biology. The hierarchical nature of these pairings, with >600 E3s and ~40 E2s in humans, necessitates that E2s cofunction with numerous ...E3 ligases partner with E2 enzymes to regulate vast eukaryotic biology. The hierarchical nature of these pairings, with >600 E3s and ~40 E2s in humans, necessitates that E2s cofunction with numerous different E3s. Here, focusing on E3s in the RING-between-RING (RBR) family and their partner UBE2L3 and UBE2D-family E2s, we report an approach to interrogate selected pathways. We screened phage-displayed libraries of structure-based E2 variants (E2Vs) to discover enzymes with enhanced affinity and specificity toward half of all RBR E3 ligases (ARIH1, ARIH2, ANKIB1, CUL9, HOIL1, HOIP, and RNF14). Collectively, these E2Vs allowed distinguishing actions of different cofunctioning E3s, obtaining high-resolution cryogenic Electron Microscopy (cryo-EM) structures of an RBR E3 in the context of a substrate-bound multiprotein complex, and profiling an endogenous RBR E3 response to an extracellular stimulus. Overall, we anticipate that E2V technology will be a generalizable tool to enable in-depth mechanistic and structural analysis of E3 ligase functions, and mapping their activity states and protein partners in cellular signaling cascades.
リンク	Proc Natl Acad Sci U S A / PubMed:41481455 / PubMed Central
手法	EM (単粒子)
解像度	2.83 - 3.23 Å
構造データ	54793 9sdx EMDB-54793: Structure of Neddylated CUL5 C-terminal region-RBX2-ARIH2~L3A2-1~Ub PDB-9sdx: Structure of RBR binding E2 variant crosslinked with NEDD8-CUL5-RBX2 bound ARIH2 and Ub 手法: EM (単粒子) / 解像度: 2.97 Å 54794 9sdy EMDB-54794, PDB-9sdy: Structure of RBR E2 variant binding to CUL5-RBX2 bound ARIH2 手法: EM (単粒子) / 解像度: 3.06 Å EMDB-54795: Cryo-EM map of focus refined ASB9-Elob/C-CKB bound to Nedd8-CUL5-RBX2-ARIH2-L3A2-1 手法: EM (単粒子) / 解像度: 2.83 Å EMDB-54892: consensus map of Neddylated CUL5-ARIH2-L3A2-1 bound to ASB9-EloB/C-CKB 手法: EM (単粒子) / 解像度: 3.06 Å EMDB-54893: Focus refined map of Neddylated CUL5-ARIH2-L3A2-1 bound to ASB9-EloB/C-CKB, focus refined on ARIH2-L3A2-1 手法: EM (単粒子) / 解像度: 3.23 Å EMDB-54933: Consensus Map of Neddylated CUL5 C-terminal region-RBX2-ARIH2~L3A2-1~Ub 手法: EM (単粒子) / 解像度: 2.97 Å EMDB-54934: Focus refined map of Neddylated CUL5 C-terminal region-RBX2-ARIH2~L3A2-1~Ub 手法: EM (単粒子) / 解像度: 3.17 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-SY8: 5-azanylpentan-2-one
由来	homo sapiens (ヒト) synthetic construct (人工物)
キーワード	LIGASE / Complex