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- SASDF25: R16-24 del45-55 human dystrophin fragment (Human dystrophin centr... -

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Basic information

Entry
Database: SASBDB / ID: SASDF25
SampleR16-24 del45-55 human dystrophin fragment
  • Human dystrophin central domain R16-24 del45-55 fragment (protein)
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 / structural constituent of muscle / muscle organ development / myosin binding / muscle cell cellular homeostasis / maintenance of blood-brain barrier / nitric-oxide synthase binding / negative regulation of peptidyl-serine phosphorylation / Non-integrin membrane-ECM interactions / neuron development / regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / cardiac muscle contraction / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / skeletal muscle tissue development / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / sarcolemma / structural constituent of cytoskeleton / Z disc / positive regulation of neuron projection development / 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 / 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. / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Calponin homology (CH) domain / 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

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Models

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Sample

SampleName: R16-24 del45-55 human dystrophin fragment
BufferName: NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycérol 2% / pH: 7.5
Entity #1558Type: protein
Description: Human dystrophin central domain R16-24 del45-55 fragment
Formula weight: 58.102 / Num. of mol.: 1 / References: UniProt: P11532
Sequence: MSYYHHHHHH DYDIPTTENL YFOGAMGRSL VPRGSLEISY VPSTYLTEIT HVSQALLEVE QLLNAPDLCA KDFEDLFKQE ESLKNIKDSL QQSSGRIDII HSKKTAALQS ATPVERVKLQ EALSQLDFQW EKVNKMYKDR QGRFDRSVEK WRRFHYDIKI FNQWLTEAEQ ...Sequence:
MSYYHHHHHH DYDIPTTENL YFOGAMGRSL VPRGSLEISY VPSTYLTEIT HVSQALLEVE QLLNAPDLCA KDFEDLFKQE ESLKNIKDSL QQSSGRIDII HSKKTAALQS ATPVERVKLQ EALSQLDFQW EKVNKMYKDR QGRFDRSVEK WRRFHYDIKI FNQWLTEAEQ FLRKTQIPEN WEHAKYKWYL KDLQGEIEAH TDVYHNLDEN SQKILRSLEG SDDAVLLQRR LDNMNFKWSE LRKKSLNIRS HLEASSDQWK RLHLSLQELL VWLQLKDDEL SRQAPIGGDF PAVQKQNDVH RAFKRELKTK EPVIMSTLET VRIFLTEQPL EGLEKLYQEP RELPPEERAQ NVTRLLRKQA EEVNTEWEKL NLHSADWQRK IDETLERLQE LQEATDELDL KLRQAEVIKG SWQPVGDLLI DSLQDHLEKV KALRGEIAPL KENVSHVNDL ARQLTTLGIQ LSPYNLSTLE DLNTRWKLLQ VAVEDRVRQL HE

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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: R16-24 del45-55 human dystrophin fragment / Measurement date: Sep 28, 2017 / Cell temperature: 20 °C / Exposure time: 1.5 sec. / Number of frames: 21 / Unit: 1/A /
MinMax
Q0.0068 0.6048
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 441 /
MinMax
Q0.01185 0.2599
P(R) point9 449
R0 183
Result
Experimental MW: 61 kDa / D max: 18.3 / Type of curve: sec
Comments: SEC-SAXS was performed at 20°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.2 mL/min; Sample injection concentration: ~8 mg/mL; Injection volume: ...Comments: SEC-SAXS was performed at 20°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.2 mL/min; Sample injection concentration: ~8 mg/mL; Injection volume: 50μL. The data were collected through the SEC peak of the protein as a series of 21 x 1.5 second exposures. The experimental molecular weight was determined from the volume of correlation, Vc.
P(R)Guinier
Forward scattering, I01.074 1.03
Radius of gyration, Rg5.17 nm4.67 nm

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