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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 / synaptic signaling / cardiac muscle cell action potential / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / positive regulation of sodium ion transmembrane transporter activity / dystrophin-associated glycoprotein complex ...regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / synaptic signaling / cardiac muscle cell action potential / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / positive regulation of sodium ion transmembrane transporter activity / dystrophin-associated glycoprotein complex / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / peptide biosynthetic process / cell-substrate junction / motile cilium assembly / dystroglycan binding / vinculin binding / muscle cell development / costamere / neuron projection terminus / Striated Muscle Contraction / filopodium membrane / muscle organ development / structural constituent of muscle / muscle cell cellular homeostasis / myosin binding / maintenance of blood-brain barrier / nitric-oxide synthase binding / negative regulation of peptidyl-serine phosphorylation / Non-integrin membrane-ECM interactions / neuron development / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / cardiac muscle contraction / skeletal muscle tissue development / regulation of ryanodine-sensitive calcium-release channel activity / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / protein localization / structural constituent of cytoskeleton / sarcolemma / positive regulation of neuron projection development / Z disc / 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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