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- SASDFZ4: R16-24 human dystrophin fragment (Human dystrophin central domain... -
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Open data
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Basic information
Entry | ![]() |
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![]() | R16-24 human dystrophin fragment
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Function / homology | ![]() 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 ...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 Similarity search - Function |
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Structure visualization
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: R16-24 human dystrophin fragment |
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Buffer | Name: NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycérol 2% / pH: 7.5 |
Entity #1557 | Type: protein Description: Human dystrophin central domain R16-24 fragment Formula weight: 126.616 / 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 KELQDGIGQR QTVVRTLNAT GEEIIQQSSK TDASILQEKL GSLNLRWQEV CKQLSDRKKR LEEQKNILSE FQRDLNEFVL WLEEADNIAS IPLEPGKEQQ LKEKLEQVKL LVEELPLRQA GILKQLNETG GPVLVSAPIS PEEQDKLENK LKQTNLQWIK VSRALPEKQG EIEAQIKDLG QLEKKLEDLE EQLNHLLLWL SPIRNQLEIY NQPNQEGPFD VQETEIAVQA KQPDVEEILS KGQHLYKEKP ATQPVKRKLE DLSSEWKAVN RLLQELRAKQ PDLAPGLTTI GASPTQTVTL VTQPVVTKET AISKLEMPSS LMLEVPALAD FNRAWTELTD WLSLLDQVIK SQRVMVGDLE DINEMIIKQK ATMQDLEQRR PQLEELITAA QNLKNKTSNQ EARTIITDRI ERIQNQWDEV QEHLQNRRQQ LNEMLKDSTQ WLEAKEEAEQ VLGQARAKLE SWKEGPYTVD AIQKKITETK QLAKDLRQWQ TNVDVANDLA LKLLRDYSAD DTRKVHMITE NINASWRSIH KRVSEREAAL EETHRLLQQF PLDLEKFLAW LTEAETTANV LQDATRKERL LEDSKGVKEL MKQWQDLQGE IEAHTDVYHN LDENSQKILR SLEGSDDAVL LQRRLDNMNF KWSELRKKSL NIRSHLEASS DQWKRLHLSL QELLVWLQLK DDELSRQAPI GGDFPAVQKQ NDVHRAFKRE LKTKEPVIMS TLETVRIFLT EQPLEGLEKL YQEPRELPPE ERAQNVTRLL RKQAEEVNTE WEKLNLHSAD WQRKIDETLE RLQELQEATD ELDLKLRQAE VIKGSWQPVG DLLIDSLQDH LEKVKALRGE IAPLKENVSH VNDLARQLTT LGIQLSPYNL STLEDLNTRW KLLQVAVEDR VRQLHE |
-Experimental information
Beam | Instrument name: SOLEIL SWING ![]() ![]() | ||||||||||||
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Detector | Name: AVIEX PCCD170170 / Type: CCD | ||||||||||||
Scan |
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Distance distribution function P(R) |
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Result | Comments: SEC-SAXS was performed at 20°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 4.5 mg/mL; Injection ...Comments: SEC-SAXS was performed at 20°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 4.5 mg/mL; Injection volume: 50μL. The data were collected through the SEC peak of the protein as a series of 38 x 0.75 second exposures. The experimental molecular weight was determined from SEC-MALS (130 kDa).
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