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- SASDDL9: Conformation of R1-3 human dystrophin fragment in interaction wit... -

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Basic information

Entry
Database: SASBDB / ID: SASDDL9
SampleConformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
  • R1-3 human dystrophin fragment (protein), R1-3, Homo sapiens
Function / homology
Function and homology information


regulation of muscle system process / regulation of cellular response to growth factor stimulus / syntrophin complex / cardiac muscle cell action potential / synaptic signaling / dystrophin-associated glycoprotein complex / cell-substrate junction / motile cilium assembly / peptide biosynthetic process / dystroglycan binding ...regulation of muscle system process / regulation of cellular response to growth factor stimulus / syntrophin complex / cardiac muscle cell action potential / synaptic signaling / dystrophin-associated glycoprotein complex / cell-substrate junction / motile cilium assembly / peptide biosynthetic process / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / vinculin binding / camera-type eye development / regulation of sodium ion transmembrane transport / costamere / Formation of the dystrophin-glycoprotein complex (DGC) / muscle cell development / regulation of calcium ion transmembrane transport / Striated Muscle Contraction / muscle cell cellular homeostasis / filopodium membrane / muscle organ development / structural constituent of muscle / maintenance of blood-brain barrier / myosin binding / neuron projection terminus / nitric-oxide synthase binding / regulation of skeletal muscle contraction / skeletal muscle tissue development / Non-integrin membrane-ECM interactions / neuron development / response to muscle stretch / cardiac muscle contraction / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / positive regulation of neuron differentiation / regulation of heart rate / filopodium / positive regulation of neuron projection development / sarcolemma / Z disc / structural constituent of cytoskeleton / intracellular protein localization / actin binding / protein-containing complex assembly / cytoskeleton / postsynaptic membrane / membrane raft / synapse / cell surface / protein-containing complex / zinc ion binding / nucleus / plasma membrane / cytosol
Similarity search - Function
Dystrophin/utrophin / EF-hand domain, type 1 / EF-hand domain, type 2 / EF hand / EF-hand / : / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Spectrin repeats ...Dystrophin/utrophin / EF-hand domain, type 1 / EF-hand domain, type 2 / EF hand / EF-hand / : / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Spectrin repeats / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Zinc finger ZZ-type signature. / Calponin homology (CH) domain / Zinc finger, ZZ type / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / EF-hand domain pair
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationDate: 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
  • Sophie Combet (LLB, UMR12 CEA/CNRS)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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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

SampleName: Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
Specimen concentration: 4.2 mg/ml
BufferName: 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 #1162Name: 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

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Experimental information

BeamInstrument name: ILL D22 / City: Grenoble / 国: France / Type of source: neutron source / Wavelength: 0.6 Å / Dist. spec. to detc.: 1.4 mm
DetectorName: 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 /
MinMax
Q0.0065 0.6143
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 115 /
MinMax
Q0.01187 0.2505
P(R) point5 119
R0 248
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.
ExperimentalPorod
MW46 kDa-
Volume-100 nm3

P(R)GuinierGuinier error
Forward scattering, I00.1683 0.175 -
Radius of gyration, Rg6.08 nm6.2 nm4

MinMax
D-24.8
Guinier point1 13

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