+データを開く
-基本情報
登録情報 | データベース: SASBDB / ID: SASDB46 |
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試料 | Glycosylated Myelin-associated glycoprotein immunoglobulin domains 1-3
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機能・相同性 | 機能・相同性情報 mesaxon / Axonal growth inhibition (RHOA activation) / Basigin interactions / ganglioside GT1b binding / central nervous system myelination / sialic acid binding / myelin sheath adaxonal region / central nervous system myelin formation / positive regulation of myelination / negative regulation of axon extension ...mesaxon / Axonal growth inhibition (RHOA activation) / Basigin interactions / ganglioside GT1b binding / central nervous system myelination / sialic acid binding / myelin sheath adaxonal region / central nervous system myelin formation / positive regulation of myelination / 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 | Mus musculus (ハツカネズミ) |
引用 | ジャーナル: Nat Commun / 年: 2016 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: MolmilJmol/JSmol |
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-ダウンロードとリンク
-Data source
SASBDBのページ | SASDB46 |
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-関連構造データ
-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 #571 | 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: 8.248384 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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-試料
試料 | 名称: Glycosylated Myelin-associated glycoprotein immunoglobulin domains 1-3 試料濃度: 1.74 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 #396 | 名称: MAG / タイプ: protein / 記述: Myelin-associated glycoprotein Ig domains 1-3 / 分子量: 34.98 / 分子数: 1 / 由来: Mus musculus / 参照: UniProt: P20917 配列: GSGHWGAWMP STISAFEGTC VSIPCRFDFP DELRPAVVHG VWYFNSPYPK NYPPVVFKSR TQVVHESFQG RSRLLGDLGL RNCTLLLSTL SPELGGKYYF RGDLGGYNQY TFSEHSVLDI VNTPNIVVPP EVVAGTEVEV SCMVPDNCPE LRPELSWLGH EGLGEPTVLG ...配列: GSGHWGAWMP STISAFEGTC VSIPCRFDFP DELRPAVVHG VWYFNSPYPK NYPPVVFKSR TQVVHESFQG RSRLLGDLGL RNCTLLLSTL SPELGGKYYF RGDLGGYNQY TFSEHSVLDI VNTPNIVVPP EVVAGTEVEV SCMVPDNCPE LRPELSWLGH EGLGEPTVLG RLREDEGTWV QVSLLHFVPT REANGHRLGC QAAFPNTTLQ FEGYASLDVK YPPVIVEMNS SVEAIEGSHV SLLCGADSNP PPLLTWMRDG MVLREAVAKS LYLDLEEVTP GEDGVYACLA ENAYGQDNRT VELSVMYAAA AHHHHHH |
-実験情報
ビーム | 設備名称: ESRF BM29 / 地域: Grenoble / 国: France / 線源: X-ray synchrotron / 波長: 0.0992 Å / スペクトロメータ・検出器間距離: 2.87 mm | ||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus 1M | ||||||||||||||||||||||||||||||
スキャン | タイトル: Glycosylated Myelin-associated glycoprotein immuno 測定日: 2014年9月11日 / 保管温度: 20 °C / セル温度: 20 °C / 照射時間: 2 sec. / フレーム数: 10 / 単位: 1/nm /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 4.6 / ポイント数: 418 /
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結果 | カーブのタイプ: single_conc コメント: Myelin-associated glycoprotein (MAG) immunoglobulin domains 1-3 that should, based on the crystal structure, be monomeric.
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