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- SASDFW4: Conformation of R8-15 human dystrophin fragment (Human dystrophin... -

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Basic information

Entry
Database: SASBDB / ID: SASDFW4
SampleConformation of R8-15 human dystrophin fragment
  • Human dystrophin central domain R8-15 fragment (protein)
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 / regulation of skeletal muscle contraction / synaptic signaling / dystrophin-associated glycoprotein complex / cell-substrate junction / peptide biosynthetic process / motile cilium assembly ...regulation of muscle system process / regulation of cellular response to growth factor stimulus / syntrophin complex / cardiac muscle cell action potential / regulation of skeletal muscle contraction / synaptic signaling / dystrophin-associated glycoprotein complex / cell-substrate junction / peptide biosynthetic process / motile cilium assembly / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / vinculin binding / regulation of sodium ion transmembrane transport / Formation of the dystrophin-glycoprotein complex (DGC) / costamere / muscle cell development / regulation of calcium ion transmembrane transport / neuron projection terminus / Striated Muscle Contraction / filopodium membrane / structural constituent of muscle / muscle organ development / muscle cell cellular homeostasis / myosin binding / maintenance of blood-brain barrier / nitric-oxide synthase binding / Non-integrin membrane-ECM interactions / neuron development / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / skeletal muscle tissue development / cardiac muscle contraction / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / positive regulation of neuron projection development / sarcolemma / 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
Similarity search - Function
Dystrophin/utrophin / EF-hand domain, type 1 / EF-hand domain, type 2 / EF hand / EF-hand / : / Spectrin repeat / Spectrin repeat / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. ...Dystrophin/utrophin / EF-hand domain, type 1 / EF-hand domain, type 2 / EF hand / EF-hand / : / Spectrin repeat / Spectrin repeat / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Spectrin/alpha-actinin / Spectrin repeats / Calponin homology domain / Zinc finger ZZ-type signature. / Calponin homology (CH) domain / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Zinc finger, ZZ type / 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
Contact author
  • Raphael Dos Santos Morais (University of Lorraine)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #2888
Type: atomic / Chi-square value: 1.819
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Conformation of R8-15 human dystrophin fragment
BufferName: NaP 10 mM, NaCl 500 mM, EDTA 1 mM, Glycerol 2% / pH: 7.5
Entity #1554Type: protein / Description: Human dystrophin central domain R8-15 fragment / Formula weight: 100.208 / Num. of mol.: 1 / References: UniProt: P11532
Sequence: MSYYHHHHHH DYDIPTTENL YFQGAMDPEF DCGSRKEALK GGLEKTVSLQ KDLSEMHEWM TQAEEEYLER DFEYKTPDEL QKAVEEMKRA KEEAQQKEAK VKLLTESVNS VIAQAPPVAQ EALKKELETL TTNYQWLCTR LNGKCKTLEE VWACWHELLS YLEKANKWLN ...Sequence:
MSYYHHHHHH DYDIPTTENL YFQGAMDPEF DCGSRKEALK GGLEKTVSLQ KDLSEMHEWM TQAEEEYLER DFEYKTPDEL QKAVEEMKRA KEEAQQKEAK VKLLTESVNS VIAQAPPVAQ EALKKELETL TTNYQWLCTR LNGKCKTLEE VWACWHELLS YLEKANKWLN EVEFKLKTTE NIPGGAEEIS EVLDSLENLM RHSEDNPNQI RILAQTLTDG GVMDELINEE LETFNSRWRE LHEEAVRRQK LLEQSIQSAQ ETEKSLHLIQ ESLTFIDKQL AAYIADKVDA AQMPQEAQKI QSDLTSHEIS LEEMKKHNQG KEAAQRVLSQ IDVAQKKLQD VSMKFRLFQK PANFELRLQE SKMILDEVKM HLPALETKSV EQEVVQSQLN HCVNLYKSLS EVKSEVEMVI KTGRQIVQKK QTENPKELDE RVTALKLHYN ELGAKVTERK QQLEKCLKLS RKMRKEMNVL TEWLAATDME LTKRSAVEGM PSNLDSEVAW GKATQKEIEK QKVHLKSITE VGEALKTVLG KKETLVEDKL SLLNSNWIAV TSRAEEWLNL LLEYQKHMET FDQNVDHITK WIIQADTLLD ESEKKKPQQK EDVLKRLKAE LNDIRPKVDS TRDQAANLMA NRGDHCRKLV EPQISELNHR FAAISHRIKT GKASIPLKEL EQFNSDIQKL LEPLEAEIQQ GVNLKEEDFN KDMNEDNEGT VKELLQRGDN LQQRITDERK REEIKIKQQL LQTKHNALKD LRSQRRKKAL EISHQWYQYK RQADDLLKCL DDIEKKLASL PEPRDERKIK EIDRELQKKK EELNAVRRQA EGLSEDGAAM AVEPTQIQLS KRWREIESKF AQFRRLNFAQ

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Experimental information

BeamInstrument name: SOLEIL SWING / City: Saint-Aubin / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.1033 Å / Dist. spec. to detc.: 1.8 mm
DetectorName: AVIEX PCCD170170 / Type: CCD
Scan
Title: Conformation of R8-15 human dystrophin fragment / Measurement date: Sep 23, 2015 / Cell temperature: 15 °C / Exposure time: 1.5 sec. / Number of frames: 38 / Unit: 1/A /
MinMax
Q0.0062 0.6145
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 478 /
MinMax
Q0.00735 0.2768
P(R) point3 480
R0 360
Result
Experimental MW: 88 kDa / Type of curve: sec
Comments: SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.2 mL/min; Sample injection concentration: 4 mg/mL; Injection volume: ...Comments: SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.2 mL/min; Sample injection concentration: 4 mg/mL; Injection volume: 60μL. The data were collected through the SEC peak of the protein as a series of 38 x 1.5 second exposures. The experimental molecular weight was determined from the volume of correlation, Vc.
P(R)Guinier
Forward scattering, I00.03204 0.0327
Radius of gyration, Rg9.93 nm10.06 nm

MinMax
D-36
Guinier point1 9

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