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Yorodumi- SASDDL9: Conformation of R1-3 human dystrophin fragment in interaction wit... -
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-Basic information
Entry | Database: SASBDB / ID: SASDDL9 |
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Sample | Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
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Function / homology | Function and homology information regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / synaptic signaling / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / cardiac muscle cell action potential / 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 / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / cardiac muscle cell action potential / positive regulation of sodium ion transmembrane transporter activity / dystrophin-associated glycoprotein complex / cell-substrate junction / motile cilium assembly / peptide biosynthetic process / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / 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 / regulation of ryanodine-sensitive calcium-release channel activity / 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 / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / sarcolemma / structural constituent of cytoskeleton / positive regulation of neuron projection development / Z disc / 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 Similarity search - Function |
Biological species | Homo sapiens (human) |
Citation | Date: 2018 Aug Title: Human dystrophin structural changes upon binding to anionic membrane lipids Authors: 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 |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDDL9 |
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-Related structure data
Related structure data | C: citing same article (ref.) |
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Similar structure data |
-External links
Related items in Molecule of the Month |
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-Models
Model #2141 | Type: atomic / Chi-square value: 6.972 Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS) Specimen concentration: 4.2 mg/ml |
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Buffer | Name: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5 pH: 7.1 / Comment: pD = pH + 04 |
Entity #1162 | Name: R1-3 / Type: protein / Description: R1-3 human dystrophin fragment / Formula weight: 38.501 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P11532 Sequence: GSEVNLDRYQ TALEEVLSWL LSAEDTLQAQ GEISNDVEVV KDQFHTHEGY MMDLTAHQGR VGNILQLGSK LIGTGKLSED EETEVQEQMN LLNSRWECLR VASMEKQSNL HRVLMDLQNQ KLKELNDWLT KTEERTRKME EEPLGPDLED LKRQVQQHKV LQEDLEQEQV ...Sequence: 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 |
-Experimental information
Beam | Instrument name: ILL D22 / City: Grenoble / 国: France / Type of source: neutron source / Wavelength: 0.6 Å / Dist. spec. to detc.: 1.4 mm | ||||||||||||||||||||||||||||||
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Detector | Name: 128 linear sensitive Reuter-Stokes detector / Type: 3He multidetector / Pixsize x: 0.8 mm | ||||||||||||||||||||||||||||||
Scan | Title: Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS) Measurement date: Nov 7, 2016 / Storage temperature: 4 °C / Cell temperature: 22 °C / Unit: 1/A /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 115 /
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Result | Type of curve: single_conc Comments: 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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