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基本情報
登録情報 | データベース: SASBDB / ID: SASDB36 |
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![]() | Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant
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機能・相同性 | ![]() mesaxon / Axonal growth inhibition (RHOA activation) / Basigin interactions / ganglioside GT1b binding / central nervous system myelination / sialic acid binding / positive regulation of myelination / myelin sheath adaxonal region / central nervous system myelin formation / negative regulation of axon extension ...mesaxon / Axonal growth inhibition (RHOA activation) / Basigin interactions / ganglioside GT1b binding / central nervous system myelination / sialic acid binding / positive regulation of myelination / myelin sheath adaxonal region / central nervous system myelin formation / negative regulation of axon extension / cell-cell adhesion via plasma-membrane adhesion molecules / paranode region of axon / Schmidt-Lanterman incisure / positive regulation of astrocyte differentiation / axon regeneration / transmission of nerve impulse / negative regulation of neuron differentiation / myelination / cellular response to mechanical stimulus / negative regulation of neuron projection development / myelin sheath / carbohydrate binding / negative regulation of neuron apoptotic process / cell adhesion / membrane raft / signaling receptor binding / protein kinase binding / protein homodimerization activity / plasma membrane 類似検索 - 分子機能 |
生物種 | ![]() ![]() |
![]() | ![]() タイトル: Structural basis of myelin-associated glycoprotein adhesion and signalling. 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 / ![]() 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. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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-Data source
SASBDBのページ | ![]() |
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-関連構造データ
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外部リンク
「今月の分子」の関連する項目 |
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-モデル
モデル #570 | ![]() タイプ: atomic / ソフトウェア: Crysol (2.8.3) / ダミー原子の半径: 1.90 A / カイ2乗値: 11.888704 ![]() |
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試料
![]() | 名称: Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant 試料濃度: 2.12 mg/ml |
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バッファ | 名称: HEPES / 濃度: 20.00 mM / pH: 7.5 / 組成: 150 mM NaCl |
要素 #393 | 名称: MAG / タイプ: protein 記述: Myelin-associated glycoprotein (20-508; N406Q mutant) 分子量: 53.978 / 分子数: 1 / 由来: Mus musculus / 参照: UniProt: P20917 配列: GHWGAWMPST ISAFEGTCVS IPCRFDFPDE LRPAVVHGVW YFNSPYPKNY PPVVFKSRTQ VVHESFQGRS RLLGDLGLRN CTLLLSTLSP ELGGKYYFRG DLGGYNQYTF SEHSVLDIVN TPNIVVPPEV VAGTEVEVSC MVPDNCPELR PELSWLGHEG LGEPTVLGRL ...配列: GHWGAWMPST ISAFEGTCVS IPCRFDFPDE LRPAVVHGVW YFNSPYPKNY PPVVFKSRTQ VVHESFQGRS RLLGDLGLRN CTLLLSTLSP ELGGKYYFRG DLGGYNQYTF SEHSVLDIVN TPNIVVPPEV VAGTEVEVSC MVPDNCPELR PELSWLGHEG LGEPTVLGRL REDEGTWVQV SLLHFVPTRE ANGHRLGCQA AFPNTTLQFE GYASLDVKYP PVIVEMNSSV EAIEGSHVSL LCGADSNPPP LLTWMRDGMV LREAVAKSLY LDLEEVTPGE DGVYACLAEN AYGQDNRTVE LSVMYAPWKP TVNGTVVAVE GETVSILCST QSNPDPILTI FKEKQILATV IYESQLQLEL PAVTPEDDGE YWCVAENQYG QRATAFQLSV EFAPIILLES HCAAARDTVQ CLCVVKSNPE PSVAFELPSR NVTVNETERE FVYSERSGLL LTSILTIRGQ AQAPPRVICT SRNLYGTQSL ELPFQGAHR |
-実験情報
ビーム | 設備名称: ESRF BM29 / 地域: Grenoble / 国: France ![]() | ||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus 1M | ||||||||||||||||||||||||||||||
スキャン | 測定日: 2016年2月5日 / 保管温度: 20 °C / セル温度: 20 °C / 照射時間: 1 sec. / フレーム数: 9 / 単位: 1/nm /
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距離分布関数 P(R) |
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結果 | コメント: Myelin-associated glycoprotein (MAG) full extracellular domain (immunoglobulin domains 1-5) with an N406Q mutation that should, based on the crystal structure, enhance MAG dimerization ...コメント: Myelin-associated glycoprotein (MAG) full extracellular domain (immunoglobulin domains 1-5) with an N406Q mutation that should, based on the crystal structure, enhance MAG dimerization by removing an N-linked glycan that clashes with its symmetry mate.
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