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	Structural basis of myelin-associated glycoprotein adhesion and signalling.
ジャーナル・号・ページ	Nat Commun, Vol. 7, Page 13584, Year 2016
掲載日	2016年12月6日
著者	Matti F Pronker / Suzanne Lemstra / Joost Snijder / Albert J R Heck / Dominique M E Thies-Weesie / R Jeroen Pasterkamp / Bert J C Janssen /
PubMed 要旨	Myelin-associated glycoprotein (MAG) is a myelin-expressed cell-adhesion and bi-directional signalling molecule. MAG maintains the myelin-axon spacing by interacting with specific neuronal ...Myelin-associated glycoprotein (MAG) is a myelin-expressed cell-adhesion and bi-directional signalling molecule. MAG maintains the myelin-axon spacing by interacting with specific neuronal glycolipids (gangliosides), inhibits axon regeneration and controls myelin formation. The mechanisms underlying MAG adhesion and signalling are unresolved. We present crystal structures of the MAG full ectodomain, which reveal an extended conformation of five Ig domains and a homodimeric arrangement involving membrane-proximal domains Ig4 and Ig5. MAG-oligosaccharide complex structures and biophysical assays show how MAG engages axonal gangliosides at domain Ig1. Two post-translational modifications were identified-N-linked glycosylation at the dimerization interface and tryptophan C-mannosylation proximal to the ganglioside binding site-that appear to have regulatory functions. Structure-guided mutations and neurite outgrowth assays demonstrate MAG dimerization and carbohydrate recognition are essential for its regeneration-inhibiting properties. The combination of trans ganglioside binding and cis homodimerization explains how MAG maintains the myelin-axon spacing and provides a mechanism for MAG-mediated bi-directional signalling.
リンク	Nat Commun / PubMed:27922006 / PubMed Central
手法	SAS (X-ray synchrotron) / X線回折
解像度	2.12 - 4.3 Å
構造データ	SASDB26: Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) I473E mutant 手法: SAXS/SANS SASDB36: Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant 手法: SAXS/SANS SASDB46: Glycosylated Myelin-associated glycoprotein immunoglobulin domains 1-3 手法: SAXS/SANS SASDB55: Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5) 手法: SAXS/SANS SASDB56: Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) I473E mutant 手法: SAXS/SANS SASDB66: Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) N406Q mutant 手法: SAXS/SANS SASDB76: Deglycosylated myelin-associated glycoprotein (immunoglobulin domains 1-3) 手法: SAXS/SANS SASDBF6: Deglycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5) 手法: SAXS/SANS PDB-5lf5: Myelin-associated glycoprotein (MAG) deglycosylated full extracellular domain with co-purified ligand 手法: X-RAY DIFFRACTION / 解像度: 3.8 Å PDB-5lfr: Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3 手法: X-RAY DIFFRACTION / 解像度: 2.12 Å PDB-5lfu: Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain 手法: X-RAY DIFFRACTION / 解像度: 4.3 Å PDB-5lfv: Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3 with soaked trisaccharide ligand 手法: X-RAY DIFFRACTION / 解像度: 2.3 Å
化合物	ChemComp-MAN: alpha-D-mannopyranose / α-D-マンノピラノ-ス ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-アセチル-β-D-グルコサミン ChemComp-GOL: GLYCEROL / グリセロ-ル ChemComp-SO4: SULFATE ION / 硫酸ジアニオン ChemComp-HOH: WATER
由来	mus musculus (ハツカネズミ)
キーワード	CELL ADHESION / Myelin / Signaling / cell adhesion molecule