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- SASDFV4: Conformation of R11-15 human dystrophin fragment in interaction w... -

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Basic information

Entry
Database: SASBDB / ID: SASDFV4
SampleConformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
  • Dystrophin (R11-15 human dystrophin fragment) (protein), Dystrophin 1461-1973, Homo sapiens
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
Biological speciesHomo sapiens (human)
Contact author
  • Raphael Dos Santos Morais (University of Lorraine)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #2886
Type: dummy / Radius of dummy atoms: 2.10 A / Chi-square value: 0.676 / P-value: 0.362668
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
Specimen concentration: 5.6 mg/ml
BufferName: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O
pH: 7.1 / Comment: pD 7.5 (pH 7.1)
Entity #1527Name: Dystrophin 1461-1973 / Type: protein / Description: Dystrophin (R11-15 human dystrophin fragment) / Formula weight: 60.065 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P11532
Sequence: GSFQKPANFE QRLQESKMIL DEVKMHLPAL ETKSVEQEVV QSQLNHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK VTERKQQLEK CLKLSRKMRK EMNVLTEWLA ATDMELTKRS AVEGMPSNLD SEVAWGKATQ KEIEKQKVHL ...Sequence:
GSFQKPANFE QRLQESKMIL DEVKMHLPAL ETKSVEQEVV QSQLNHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK VTERKQQLEK CLKLSRKMRK EMNVLTEWLA ATDMELTKRS AVEGMPSNLD SEVAWGKATQ KEIEKQKVHL KSITEVGEAL KTVLGKKETL VEDKLSLLNS NWIAVTSRAE EWLNLLLEYQ KHMETFDQNV DHITKWIIQA DTLLDESEKK KPQQKEDVLK RLKAELNDIR PKVDSTRDQA ANLMANHGDH CRKLVEPQIS ELNHRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE AEIQQGVNLK EEDFNKDMNE DNEGTVKELL QRGDNLQQRI TDERKREEIK IKQQLLQTKH NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDDIEK KLASLPEPRD ERKIKEIDRE LQKKKEELNA VRRQAEGLSE DGAAMAVEPT QIQLSKRWRE IESKFAQFRR LNFAQ

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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.: 8 mm
DetectorName: 128 linear sensitive Reuter-Stokes detector / Type: 3He multidetector / Pixsize x: 0.8 mm
Scan
Title: Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
Measurement date: Nov 1, 2016 / Cell temperature: 22 °C / Exposure time: 1200 sec. / Unit: 1/A /
MinMax
Q0.0065 0.6143
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 118 /
MinMax
Q0.008739 0.2506
P(R) point2 119
R0 296
Result
Type of curve: single_conc
Comments: Data were collected at two sample detector positions: 1) 1.4 m for 5 min using a neutron wavelength of 0.6 nm and; 2) 8 m for 20 min using a neutron wavelength of 0.6 nm. Both datasets were ...Comments: Data were collected at two sample detector positions: 1) 1.4 m for 5 min using a neutron wavelength of 0.6 nm and; 2) 8 m for 20 min using a neutron wavelength of 0.6 nm. Both datasets were recorded on the same sample at 5.6 mg/mL, measured at 22 °C.
ExperimentalPorod
MW53 kDa-
Volume-231 nm3

P(R)GuinierGuinier error
Forward scattering, I00.2601 0.275 0.01
Radius of gyration, Rg7.7 nm8.1 nm0.3

MinMax
D-29.6
Guinier point2 8

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