+
データを開く
-
基本情報
| 登録情報 | ![]() | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| タイトル | Cryo-EM structure of the dystrophin glycoprotein complex | |||||||||
マップデータ | ||||||||||
試料 |
| |||||||||
キーワード | complex membrane stability signaling / STRUCTURAL PROTEIN | |||||||||
| 機能・相同性 | 機能・相同性情報dystrobrevin complex / olfactory nerve structural organization / coronary vasculature morphogenesis / sarcoglycan complex / connective tissue development / walking behavior / DAG1 core M2 glycosylations / DAG1 core M1 glycosylations / DAG1 core M3 glycosylations / establishment of blood-nerve barrier ...dystrobrevin complex / olfactory nerve structural organization / coronary vasculature morphogenesis / sarcoglycan complex / connective tissue development / walking behavior / DAG1 core M2 glycosylations / DAG1 core M1 glycosylations / DAG1 core M3 glycosylations / establishment of blood-nerve barrier / establishment of glial blood-brain barrier / Matriglycan biosynthesis on DAG1 / striated muscle cell development / dystroglycan complex / nerve maturation / muscle attachment / retrograde trans-synaptic signaling by trans-synaptic protein complex / morphogenesis of an epithelial sheet / regulation of muscle system process / regulation of cellular response to growth factor stimulus / contractile ring / nucleus localization / calcium-dependent cell-matrix adhesion / cardiac muscle cell action potential / glucose import in response to insulin stimulus / myotube cell development / vascular associated smooth muscle cell development / microtubule anchoring / Regulation of expression of SLITs and ROBOs / reactive oxygen species biosynthetic process / epithelial tube branching involved in lung morphogenesis / synaptic signaling / positive regulation of skeletal muscle acetylcholine-gated channel clustering / dystrophin-associated glycoprotein complex / laminin-1 binding / extracellular matrix assembly / matrix side of mitochondrial inner membrane / response to denervation involved in regulation of muscle adaptation / Formation of the dystrophin-glycoprotein complex (DGC) / negative regulation of synaptic transmission, cholinergic / branching involved in salivary gland morphogenesis / cell-substrate junction / Striated Muscle Contraction / neurofilament / basement membrane organization / postsynaptic specialization / peptide biosynthetic process / nerve development / photoreceptor ribbon synapse / intermediate filament cytoskeleton / synaptic assembly at neuromuscular junction / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / lamin binding / vinculin binding / myelination in peripheral nervous system / positive regulation of myelination / cellular response to cholesterol / regulation of calcium ion transmembrane transport / inhibitory synapse / morphogenesis of an epithelium / skeletal muscle tissue regeneration / regulation of sodium ion transmembrane transport / membrane organization / protein localization to synapse / costamere / protein-containing complex localization / commissural neuron axon guidance / muscle cell development / angiogenesis involved in wound healing / heart process / cardiac muscle cell development / positive regulation of cell-matrix adhesion / filopodium membrane / heparan sulfate proteoglycan binding / axon regeneration / muscle cell cellular homeostasis / node of Ranvier / inhibitory synapse assembly / cardiac muscle tissue development / negative regulation of neuron differentiation / skeletal muscle tissue development / muscle organ development / extrinsic component of cytoplasmic side of plasma membrane / cardiac muscle cell contraction / response to muscle activity / multicellular organism growth / heart contraction / structural constituent of muscle / positive regulation of Rac protein signal transduction / astrocyte projection / positive regulation of oligodendrocyte differentiation / myosin binding / regulation of synapse organization / laminin receptor activity / neuron projection terminus / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / membrane protein ectodomain proteolysis / positive regulation of protein kinase activity / response to muscle stretch 類似検索 - 分子機能 | |||||||||
| 生物種 | ![]() | |||||||||
| 手法 | 単粒子再構成法 / 解像度: 3.5 Å | |||||||||
データ登録者 | Wu JP / Yan Z / Wan L | |||||||||
| 資金援助 | 中国, 1件
| |||||||||
引用 | ジャーナル: Nature / 年: 2025タイトル: Structure and assembly of the dystrophin glycoprotein complex. 著者: Li Wan / Xiaofei Ge / Qikui Xu / Gaoxingyu Huang / Tiandi Yang / Kevin P Campbell / Zhen Yan / Jianping Wu / ![]() 要旨: The dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular ...The dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular matrix. Dysfunction of dystrophin and its associated proteins results in muscular dystrophy, a disorder characterized by progressive muscle weakness and degeneration. Despite the important roles of the DGC in physiology and pathology, its structural details remain largely unknown, hindering a comprehensive understanding of its assembly and function. Here we isolated the native DGC from mouse skeletal muscle and obtained its high-resolution structure. Our findings unveil a markedly divergent structure from the previous model of DGC assembly. Specifically, on the extracellular side, β-, γ- and δ-sarcoglycans co-fold to form a specialized, extracellular tower-like structure, which has a central role in complex assembly by providing binding sites for α-sarcoglycan and dystroglycan. In the transmembrane region, sarcoglycans and sarcospan flank and stabilize the single transmembrane helix of dystroglycan, rather than forming a subcomplex as previously proposed. On the intracellular side, sarcoglycans and dystroglycan engage in assembly with the dystrophin-dystrobrevin subcomplex through extensive interaction with the ZZ domain of dystrophin. Collectively, these findings enhance our understanding of the structural linkage across the cell membrane and provide a foundation for the molecular interpretation of many muscular dystrophy-related mutations. | |||||||||
| 履歴 |
|
-
構造の表示
| 添付画像 |
|---|
-
ダウンロードとリンク
-EMDBアーカイブ
| マップデータ | emd_39568.map.gz | 290.6 MB | EMDBマップデータ形式 | |
|---|---|---|---|---|
| ヘッダ (付随情報) | emd-39568-v30.xml emd-39568.xml | 23.5 KB 23.5 KB | 表示 表示 | EMDBヘッダ |
| FSC (解像度算出) | emd_39568_fsc.xml | 14.3 KB | 表示 | FSCデータファイル |
| 画像 | emd_39568.png | 52.9 KB | ||
| Filedesc metadata | emd-39568.cif.gz | 7.1 KB | ||
| その他 | emd_39568_half_map_1.map.gz emd_39568_half_map_2.map.gz | 285.2 MB 285.2 MB | ||
| アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-39568 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-39568 | HTTPS FTP |
-関連構造データ
| 関連構造データ | ![]() 8yt8MC C: 同じ文献を引用 ( M: このマップから作成された原子モデル |
|---|---|
| 類似構造データ | 類似検索 - 機能・相同性 F&H 検索 |
-
リンク
| EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
|---|---|
| 「今月の分子」の関連する項目 |
-
マップ
| ファイル | ダウンロード / ファイル: emd_39568.map.gz / 形式: CCP4 / 大きさ: 307.5 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
| ボクセルのサイズ | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||
| 密度 |
| ||||||||||||||||||||||||||||||||||||
| 対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
| 詳細 | EMDB XML:
|
-添付データ
-ハーフマップ: #2
| ファイル | emd_39568_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 投影像・断面図 |
| ||||||||||||
| 密度ヒストグラム |
-ハーフマップ: #1
| ファイル | emd_39568_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 投影像・断面図 |
| ||||||||||||
| 密度ヒストグラム |
-
試料の構成要素
+全体 : dystrophin glycoprotein complex, DGC
+超分子 #1: dystrophin glycoprotein complex, DGC
+分子 #1: Alpha-sarcoglycan
+分子 #2: Beta-sarcoglycan
+分子 #3: Dystrobrevin alpha
+分子 #4: Delta-sarcoglycan
+分子 #5: Dystrophin
+分子 #6: Gamma-sarcoglycan
+分子 #7: unknown segment
+分子 #8: Beta-dystroglycan
+分子 #9: Sarcospan
+分子 #14: 2-acetamido-2-deoxy-beta-D-glucopyranose
+分子 #15: CHOLESTEROL
+分子 #16: ZINC ION
+分子 #17: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phospho...
+分子 #18: CALCIUM ION
-実験情報
-構造解析
解析 | 単粒子再構成法 |
|---|---|
| 試料の集合状態 | particle |
-
試料調製
| 緩衝液 | pH: 7.4 / 詳細: 25 mM MOPS-Na, 150 mM NaCl, 2 mM CaCl2, 0.01% GDN |
|---|
-
電子顕微鏡法
| 顕微鏡 | FEI TITAN KRIOS |
|---|---|
| 撮影 | フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) 平均電子線量: 50.0 e/Å2 |
| 電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
| 電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD 最大 デフォーカス(公称値): 1.9000000000000001 µm 最小 デフォーカス(公称値): 1.4000000000000001 µm |
| 実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
+
画像解析
-原子モデル構築 1
| 精密化 | プロトコル: FLEXIBLE FIT |
|---|---|
| 得られたモデル | ![]() PDB-8yt8: |
ムービー
コントローラー
万見について




キーワード
データ登録者
中国, 1件
引用





Z (Sec.)
Y (Row.)
X (Col.)







































FIELD EMISSION GUN

