SASDDL9: Conformation of R1-3 human dystrophin fragment in interaction wit...

Basic information

• Entry: Database: SASBDB / ID: SASDDL9

Sample

Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

• R1-3 human dystrophin fragment (protein), R1-3, Homo sapiens

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 / regulation of voltage-gated calcium channel activity / synaptic signaling / 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 / muscle cell cellular homeostasis / nitric-oxide synthase binding / muscle organ development / myosin binding / maintenance of blood-brain barrier / 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 / 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

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. / 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

Component:

Dystrophin

• Biological species: Homo sapiens (human)
• Citation: Date: 2018 Aug; Title: Human dystrophin structural changes upon binding to anionic membrane lipids; Authors: Santos Morais R / Delalande O / Pérez J / Mias-Lucquin D / Lagarrigue M / Martel A / Molza A / Chéron A / Raguénès-Nicol C / Chenuel T / Bondon A / Appavou M / Le Rumeur E / Combet S

Contact author

• Sophie Combet (LLB, UMR12 CEA/CNRS)

Models

• Model #2141: ; Type: atomic / Chi-square value: 6.972; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS); Specimen concentration: 4.2 mg/ml
• Buffer: Name: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5; pH: 7.1 / Comment: pD = pH + 04

Entity #1162

Name: R1-3 / Type: protein / Description: R1-3 human dystrophin fragment / Formula weight: 38.501 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P11532
Sequence:

GSEVNLDRYQ TALEEVLSWL LSAEDTLQAQ GEISNDVEVV KDQFHTHEGY MMDLTAHQGR VGNILQLGSK LIGTGKLSED EETEVQEQMN LLNSRWECLR VASMEKQSNL HRVLMDLQNQ KLKELNDWLT KTEERTRKME EEPLGPDLED LKRQVQQHKV LQEDLEQEQV RVNSLTHMVV VVDESSGDHA TAALEEQLKV LGDRWANICR WTEDRWVLLQ DILLKWQRLT EEQCLFSAWL SEKEDAVNKI HTTGFKDQNE MLSSLQKLAV LKADLEKKKQ SMGKLYSLKQ DLLSTLKNKS VTQKTEAWLD NFARCWDNLV QKLEKSTAQI SQA

Experimental information

• Beam: Instrument name: ILL D22 / City: Grenoble / 国: France / Type of source: neutron source / Wavelength: 0.6 Å / Dist. spec. to detc.: 1.4 mm
• Detector: Name: 128 linear sensitive Reuter-Stokes detector / Type: 3He multidetector / Pixsize x: 0.8 mm

Scan

Title: Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
Measurement date: Nov 7, 2016 / Storage temperature: 4 °C / Cell temperature: 22 °C / Unit: 1/A /

	Min	Max
Q	0.0065	0.6143

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 115 /

	Min	Max
Q	0.01187	0.2505
P(R) point	5	119
R	0	248

Result

Type of curve: single_conc
Comments: The sample-to-detector distance (collimation distance) and exposure times used were: 1.4 m (2.8m), 5 min and; 8m (8 m), 20 min. The CRYSON ill.res file is included in the full entry zip archive.

	Experimental	Porod
MW	46 kDa	-
Volume	-	100 nm3

	P(R)	Guinier	Guinier error
Forward scattering, I0	0.1683	0.175	-
Radius of gyration, Rg	6.08 nm	6.2 nm	4

	Min	Max
D	-	24.8
Guinier point	1	13