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データを開く
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基本情報
登録情報 | データベース: SASBDB / ID: SASDDL9 |
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![]() | Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
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機能・相同性 | ![]() regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / negative regulation of peptidyl-cysteine S-nitrosylation / regulation of voltage-gated calcium channel activity / synaptic signaling / cardiac muscle cell action potential / dystrophin-associated glycoprotein complex / positive regulation of sodium ion transmembrane transporter activity ...regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / negative regulation of peptidyl-cysteine S-nitrosylation / regulation of voltage-gated calcium channel activity / synaptic signaling / cardiac muscle cell action potential / dystrophin-associated glycoprotein complex / positive regulation of sodium ion transmembrane transporter activity / cell-substrate junction / motile cilium assembly / peptide biosynthetic process / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / Formation of the dystrophin-glycoprotein complex (DGC) / vinculin binding / costamere / muscle cell development / neuron projection terminus / Striated Muscle Contraction / filopodium membrane / structural constituent of muscle / muscle cell cellular homeostasis / nitric-oxide synthase binding / muscle organ development / myosin binding / maintenance of blood-brain barrier / Non-integrin membrane-ECM interactions / regulation of ryanodine-sensitive calcium-release channel activity / neuron development / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / skeletal muscle tissue development / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / cardiac muscle contraction / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / sarcolemma / positive regulation of neuron projection development / structural constituent of cytoskeleton / Z disc / intracellular protein localization / actin binding / protein-containing complex assembly / postsynaptic membrane / cytoskeleton / membrane raft / synapse / cell surface / protein-containing complex / zinc ion binding / nucleus / plasma membrane / cytosol 類似検索 - 分子機能 |
生物種 | ![]() |
![]() | ![]() タイトル: Human dystrophin structural changes upon binding to anionic membrane lipids 著者: Santos Morais R / Delalande O / Pérez J / Mias-Lucquin D / Lagarrigue M / Martel A / Molza A / Chéron A / Raguénès-Nicol C / Chenuel T / Bondon A / Appavou M / Le Rumeur E / Combet S |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
-モデル
モデル #2141 | ![]() タイプ: atomic / カイ2乗値: 6.972 ![]() |
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試料
![]() | 名称: Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS) 試料濃度: 4.2 mg/ml |
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バッファ | 名称: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5 pH: 7.1 / コメント: pD = pH + 04 |
要素 #1162 | 名称: R1-3 / タイプ: protein / 記述: R1-3 human dystrophin fragment / 分子量: 38.501 / 分子数: 1 / 由来: Homo sapiens / 参照: UniProt: P11532 配列: GSEVNLDRYQ TALEEVLSWL LSAEDTLQAQ GEISNDVEVV KDQFHTHEGY MMDLTAHQGR VGNILQLGSK LIGTGKLSED EETEVQEQMN LLNSRWECLR VASMEKQSNL HRVLMDLQNQ KLKELNDWLT KTEERTRKME EEPLGPDLED LKRQVQQHKV LQEDLEQEQV ...配列: GSEVNLDRYQ TALEEVLSWL LSAEDTLQAQ GEISNDVEVV KDQFHTHEGY MMDLTAHQGR VGNILQLGSK LIGTGKLSED EETEVQEQMN LLNSRWECLR VASMEKQSNL HRVLMDLQNQ KLKELNDWLT KTEERTRKME EEPLGPDLED LKRQVQQHKV LQEDLEQEQV RVNSLTHMVV VVDESSGDHA TAALEEQLKV LGDRWANICR WTEDRWVLLQ DILLKWQRLT EEQCLFSAWL SEKEDAVNKI HTTGFKDQNE MLSSLQKLAV LKADLEKKKQ SMGKLYSLKQ DLLSTLKNKS VTQKTEAWLD NFARCWDNLV QKLEKSTAQI SQA |
-実験情報
ビーム | 設備名称: ILL D22 / 地域: Grenoble / 国: France ![]() | ||||||||||||||||||||||||||||||
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検出器 | 名称: 128 linear sensitive Reuter-Stokes detector / タイプ: 3He multidetector / Pixsize x: 0.8 mm | ||||||||||||||||||||||||||||||
スキャン | 測定日: 2016年11月7日 / 保管温度: 4 °C / セル温度: 22 °C / 単位: 1/A /
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距離分布関数 P(R) |
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結果 | コメント: The sample-to-detector distance (collimation distance) and exposure times used were: 1.4 m (2.8m), 5 min and; 8m (8 m), 20 min. The CRYSON ill.res file is included in the full entry zip archive.
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