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

Basic information

• Entry: Database: SASBDB / ID: SASDFW4

Sample

Conformation of R8-15 human dystrophin fragment

• Human dystrophin central domain R8-15 fragment (protein)

Function / homology

Function:

regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / negative regulation of peptidyl-cysteine S-nitrosylation / synaptic signaling / regulation of voltage-gated calcium channel activity / cardiac muscle cell action potential / dystrophin-associated glycoprotein complex / positive regulation of sodium ion transmembrane transporter activity / cell-substrate junction / motile cilium assembly / peptide biosynthetic process / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / Formation of the dystrophin-glycoprotein complex (DGC) / vinculin binding / costamere / muscle cell development / neuron projection terminus / Striated Muscle Contraction / filopodium membrane / structural constituent of muscle / nitric-oxide synthase binding / muscle cell cellular homeostasis / muscle organ development / maintenance of blood-brain barrier / myosin binding / 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 / skeletal muscle tissue development / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / cardiac muscle contraction / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / sarcolemma / positive regulation of neuron projection development / structural constituent of cytoskeleton / 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

Domain/homology:

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

Component:

Dystrophin

Contact author

• Raphael Dos Santos Morais (University of Lorraine)

Models

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

Sample

• Sample: Name: Conformation of R8-15 human dystrophin fragment
• Buffer: Name: NaP 10 mM, NaCl 500 mM, EDTA 1 mM, Glycerol 2% / pH: 7.5

Entity #1554

Type: 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 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

Experimental information

• Beam: Instrument 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
• Detector: Name: 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 /

	Min	Max
Q	0.0062	0.6145

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 478 /

	Min	Max
Q	0.00735	0.2768
P(R) point	3	480
R	0	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: 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, I0	0.03204	0.0327
Radius of gyration, Rg	9.93 nm	10.06 nm

	Min	Max
D	-	36
Guinier point	1	9