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- SASDFX4: Conformation of R11-19 human dystrophin fragment (Human dystrophi... -

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Basic information

Entry
Database: SASBDB / ID: SASDFX4
SampleConformation of R11-19 human dystrophin fragment
  • Human dystrophin central domain R11-19 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 / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / 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 / regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / neuron development / 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 / 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
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. / Zinc finger, ZZ type / Calponin homology (CH) domain / 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 #2932
Type: atomic / Chi-square value: 12.122
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Conformation of R11-19 human dystrophin fragment
BufferName: NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycerol 2% / pH: 7.5
Entity #1574Type: protein
Description: Human dystrophin central domain R11-19 fragment
Formula weight: 116.685 / Num. of mol.: 1 / References: UniProt: P11532
Sequence: MSYYHHHHHH DYDIPTTENL YFQGAMGRSL VPRGSSFQKP ANFEQRLQES KMILDEVKMH LPALETKSVE QEVVQSQLNH CVNLYKSLSE VKSEVEMVIK TGRQIVQKKQ TENPKELDER VTALKLHYNE LGAKVTERKQ QLEKCLKLSR KMRKEMNVLT EWLAATDMEL ...Sequence:
MSYYHHHHHH DYDIPTTENL YFQGAMGRSL VPRGSSFQKP ANFEQRLQES KMILDEVKMH LPALETKSVE QEVVQSQLNH CVNLYKSLSE VKSEVEMVIK TGRQIVQKKQ TENPKELDER VTALKLHYNE LGAKVTERKQ QLEKCLKLSR KMRKEMNVLT EWLAATDMEL TKRSAVEGMP SNLDSEVAWG KATQKEIEKQ KVHLKSITEV GEALKTVLGK KETLVEDKLS LLNSNWIAVT SRAEEWLNLL LEYQKHMETF DQNVDHITKW IIQADTLLDE SEKKKPQQKE DVLKRLKAEL NDIRPKVDST RDQAANLMAN RHDHCRKLVE PQISELNHRF AAISHRIKTG KASIPLKELE QFNSDIQKLL EPLEAEIQQG VNLKEEDFNK DMNEDNEGTV KELLQRGDNL QQRITDERKR EEIKIKQQLL QTKHNALKDL RSQRRKKALE ISHQWYQYKR QADDLLKCLD DIEKKLASLP EPRDERKIKE IDRELQKKKE ELNAVRRQAE GLSEDGAAMA VEPTQIQLSK RWREIESKFA QFRRLNFAQI HTVREETMMV MTEDMPLEIS YVPSTYLTEI THVSQALLEV EQLLNAPDLC AKDFEDLFKQ EESLKNIKDS LQQSSGRIDI IHSKKTAALQ SATPVERVKL QEALSQLDFQ WEKVNKMYKD RQGRFDRSVE KWRRFHYDIK IFNQWLTEAE QFLRKTQIPE NWEHAKYKWY LKELQDGIGQ RQTVVRTLNA TGEEIIQQSS KTDASILQEK LGSLNLRWQE VCKQLSDRKK RLEEQKNILS EFQRDLNEFV LWLEEADNIA SIPLEPGKEQ QLKEKLEQVK LLVEELPLRQ GRILKQLNET GGPVLVSAPI SPEEQDKLEN KLKQTNLQWI KVSRALPEKQ GEIEAQIKDL GQLEKKLEDL EEQLNHLLLW LSPIRNQLEI YNQPNQEGPF DVQETEIAVQ AKQPDVEEIL SKGQHLYKEK PATQPVKRKL EDLSSEWKAV NRLLQEL

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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 R11-19 human dystrophin fragment / Measurement date: May 11, 2017 / Cell temperature: 15 °C / Exposure time: 0.75 sec. / Number of frames: 21 / Unit: 1/A /
MinMax
Q0.0062 0.6143
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 349 /
MinMax
Q0.006762 0.2028
P(R) point1 349
R0 375
Result
Type of curve: sec
Comments: SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500A (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 4.5 mg/mL; Injection volume: ...Comments: SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500A (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 4.5 mg/mL; Injection volume: 70 μL. 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.
ExperimentalPorod
MW120 kDa-
Volume-513 nm3

P(R)GuinierGuinier error
Forward scattering, I01.08 1.08 0.01
Radius of gyration, Rg9.14 nm8.83 nm0.13

MinMax
D-37.5
Guinier point1 11

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