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	Effect of phosphorylation barcodes on arrestin binding to a chemokine receptor.
ジャーナル・号・ページ	Nature, Vol. 643, Issue 8070, Page 280-287, Year 2025
掲載日	2025年5月21日
著者	Qiuyan Chen / Christopher T Schafer / Somnath Mukherjee / Kai Wang / Martin Gustavsson / James R Fuller / Katelyn Tepper / Thomas D Lamme / Yasmin Aydin / Parth Agrawal / Genki Terashi / Xin-Qiu Yao / Daisuke Kihara / Anthony A Kossiakoff / Tracy M Handel / John J G Tesmer /
PubMed 要旨	Unique phosphorylation 'barcodes' installed in different regions of an active seven-transmembrane receptor by different G-protein-coupled receptor (GPCR) kinases (GRKs) have been proposed to promote ...Unique phosphorylation 'barcodes' installed in different regions of an active seven-transmembrane receptor by different G-protein-coupled receptor (GPCR) kinases (GRKs) have been proposed to promote distinct cellular outcomes, but it is unclear whether or how arrestins differentially engage these barcodes. Here, to address this, we developed an antigen-binding fragment (Fab7) that recognizes both active arrestin2 (β-arrestin1) and arrestin3 (β-arrestin2) without interacting with bound receptor polypeptides. We used Fab7 to determine the structures of both arrestins in complex with atypical chemokine receptor 3 (ACKR3) phosphorylated in different regions of its C-terminal tail by either GRK2 or GRK5 (ref. ). The GRK2-phosphorylated ACKR3 resulted in more heterogeneous 'tail-mode' assemblies, whereas phosphorylation by GRK5 resulted in more rigid 'ACKR3-adjacent' assemblies. Unexpectedly, the finger loops of both arrestins engaged the micelle surface rather than the receptor intracellular pocket, with arrestin3 being more dynamic, partly because of its lack of a membrane-anchoring motif. Thus, both the region of the barcode and the arrestin isoform involved can alter the structure and dynamics of GPCR-arrestin complexes, providing a possible mechanistic basis for unique downstream cellular effects, such as the efficiency of chemokine scavenging and the robustness of arrestin binding in ACKR3.
リンク	Nature / PubMed:40399676 / PubMed Central
手法	EM (単粒子)
解像度	3.0 - 6.9 Å
構造データ	41289 8tii EMDB-41289, PDB-8tii: Human ACKR3 phosphorylated by GRK2 in complex with Arrestin2 in nanodisc 手法: EM (単粒子) / 解像度: 3.0 Å EMDB-41290: Human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 手法: EM (単粒子) / 解像度: 3.9 Å EMDB-41291: Human ACKR3 phosphorylated by GRK2 in complex with Arrestin3 手法: EM (単粒子) / 解像度: 6.9 Å EMDB-41292: Human ACKR3 with C tail extended by 12 glycines phosphorylated by GRK5 in complex with Arrestin2 手法: EM (単粒子) / 解像度: 3.8 Å 41295 8til EMDB-41295, PDB-8til: Human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 reconstructed without receptor/micelle 手法: EM (単粒子) / 解像度: 3.8 Å 41296 8tin EMDB-41296, PDB-8tin: Human ACKR3 phosphorylated by GRK2 in complex with Arrestin3 reconstructed without receptor/micelle 手法: EM (単粒子) / 解像度: 4.0 Å 41297 8tio EMDB-41297, PDB-8tio: Human ACKR3 with C tail extended by 12 glycines phosphorylated by GRK5 in complex with Arrestin2 reconstructed without receptor/micelle 手法: EM (単粒子) / 解像度: 3.6 Å 43277 8vj9 EMDB-43277: cryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant with the C edge loop from Arrestin2 inserted PDB-8vj9: CryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant with the C edge loop from Arrestin2 inserted 手法: EM (単粒子) / 解像度: 3.3 Å 47700 9e82 EMDB-47700, PDB-9e82: ACKR3 phosphorylated by GRK5 in complex with arrestin2 and Fab7 手法: EM (単粒子) / 解像度: 3.4 Å EMDB-49564: cryoEM structure of human ACKR3 phosphorylated by GRK2 in complex with Arr2 手法: EM (単粒子) / 解像度: 4.1 Å
化合物	ChemComp-CLR: CHOLESTEROL / コレステロ-ル
由来	bos taurus (ウシ) synthetic construct (人工物) homo sapiens (ヒト)
キーワード	SIGNALING PROTEIN/IMMUNE SYSTEM / complex / GPCR / arrestin / signaling / SIGNALING PROTEIN-IMMUNE SYSTEM complex