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	Molecular basis of promiscuous chemokine binding and structural mimicry at the C-X-C chemokine receptor, CXCR2.
ジャーナル・号・ページ	Mol Cell, Vol. 85, Issue 5, Page 976-988.e9, Year 2025
掲載日	2025年3月6日
著者	Shirsha Saha / Fumiya K Sano / Saloni Sharma / Manisankar Ganguly / Sudha Mishra / Annu Dalal / Hiroaki Akasaka / Takaaki A Kobayashi / Nashrah Zaidi / Divyanshu Tiwari / Nabarun Roy / Manish K Yadav / Nilanjana Banerjee / Sayantan Saha / Samanwita Mohapatra / Yuzuru Itoh / Andy Chevigné / Ramanuj Banerjee / Wataru Shihoya / Osamu Nureki / Arun K Shukla /
PubMed 要旨	Selectivity of natural agonists for their cognate receptors is a hallmark of G-protein-coupled receptors (GPCRs); however, this selectivity often breaks down at the chemokine receptors. Chemokines ...Selectivity of natural agonists for their cognate receptors is a hallmark of G-protein-coupled receptors (GPCRs); however, this selectivity often breaks down at the chemokine receptors. Chemokines often display promiscuous binding to chemokine receptors, but the underlying molecular determinants remain mostly elusive. Here, we perform a comprehensive transducer-coupling analysis, testing all known C-X-C chemokines on every C-X-C type chemokine receptor to generate a global fingerprint of the selectivity and promiscuity encoded within this system. Taking lead from this, we determine cryoelectron microscopy (cryo-EM) structures of the most promiscuous receptor, C-X-C chemokine receptor 2 (CXCR2), in complex with several chemokines. These structural snapshots elucidate the details of ligand-receptor interactions, including structural motifs, which are validated using mutagenesis and functional experiments. We also observe that most chemokines position themselves on CXCR2 as a dimer while CXCL6 exhibits a monomeric binding pose. Taken together, our findings provide the molecular basis of chemokine promiscuity at CXCR2 with potential implications for developing therapeutic molecules.
リンク	Mol Cell / PubMed:39978339 / PubMed Central
手法	EM (単粒子)
解像度	2.8 - 3.71 Å
構造データ	38719 8xvu EMDB-38719, PDB-8xvu: Structure of CXCR2 bound to CXCL2 (Ligand-receptor focused map) 手法: EM (単粒子) / 解像度: 3.09 Å 38732 8xwa EMDB-38732, PDB-8xwa: Structure of CXCR2 bound to CXCL1 (Ligand-receptor focused map) 手法: EM (単粒子) / 解像度: 3.48 Å 38734 8xwf EMDB-38734, PDB-8xwf: Structure of CXCR2 bound to CXCL3 (Ligand-receptor focused map) 手法: EM (単粒子) / 解像度: 3.65 Å 38738 8xwm EMDB-38738, PDB-8xwm: Structure of CXCR2 bound to CXCL6 (Ligand-receptor focused map) 手法: EM (単粒子) / 解像度: 3.71 Å 38739 8xwn EMDB-38739, PDB-8xwn: Structure of CXCR2 bound to CXCL8 (Ligand-receptor focused map) 手法: EM (単粒子) / 解像度: 3.29 Å 38742 8xws EMDB-38742, PDB-8xws: Structure of CXCR2 bound to CXCL5 (Ligand-receptor focused map) 手法: EM (単粒子) / 解像度: 3.06 Å 38743 8xwv EMDB-38743, PDB-8xwv: Structure of CXCR2 bound to CXCL1 (CXCR2-CXCL1-Go Full map) 手法: EM (単粒子) / 解像度: 3.07 Å 38744 8xx3 EMDB-38744, PDB-8xx3: Structure of CXCR2 bound to CXCL3 (CXCR2-CXCL3-Go Full map) 手法: EM (単粒子) / 解像度: 3.38 Å 38747 8xx6 EMDB-38747, PDB-8xx6: Structure of CXCR2 bound to CXCL8 (CXCR2-CXCL8-Go Full map) 手法: EM (単粒子) / 解像度: 2.99 Å 38748 8xx7 EMDB-38748, PDB-8xx7: Structure of CXCR2 bound to CXCL5 (CXCR2-CXCL5-Go Full map) 手法: EM (単粒子) / 解像度: 3.32 Å 38749 8xxh EMDB-38749, PDB-8xxh: Structure of CXCR2 bound to CXCL2 (CXCR2-CXCL2-Go Full map) 手法: EM (単粒子) / 解像度: 2.8 Å 38759 8xxr EMDB-38759, PDB-8xxr: Structure of CXCR2 bound to CXCL6 (CXCR2-CXCL6-Go Full map) 手法: EM (単粒子) / 解像度: 3.17 Å 38764 8xxx EMDB-38764, PDB-8xxx: Structure of CXCR2 bound to CXCL6 (Composite map) 手法: EM (単粒子) / 解像度: 3.17 Å
由来	homo sapiens (ヒト) mus musculus (ハツカネズミ)
キーワード	SIGNALING PROTEIN/IMMUNE SYSTEM / GPCR / Arrestin / SIGNALING PROTEIN-IMMUNE SYSTEM complex