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- SASDEQ7: Filamin A Ig-like domains 3-5 (FLNa3-5) (Filamin A Ig-like domain... -

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Basic information

Entry
Database: SASBDB / ID: SASDEQ7
SampleFilamin A Ig-like domains 3-5 (FLNa3-5)
  • Filamin A Ig-like domains 3-5 (protein), FLNa3-5, Homo sapiens
Function / homology
Function and homology information


regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / Myb complex / glycoprotein Ib-IX-V complex / adenylate cyclase-inhibiting dopamine receptor signaling pathway / formation of radial glial scaffolds / positive regulation of integrin-mediated signaling pathway / cytoplasmic sequestering of protein / tubulin deacetylation ...regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / Myb complex / glycoprotein Ib-IX-V complex / adenylate cyclase-inhibiting dopamine receptor signaling pathway / formation of radial glial scaffolds / positive regulation of integrin-mediated signaling pathway / cytoplasmic sequestering of protein / tubulin deacetylation / actin crosslink formation / blood coagulation, intrinsic pathway / protein localization to bicellular tight junction / OAS antiviral response / positive regulation of actin filament bundle assembly / positive regulation of neuron migration / positive regulation of potassium ion transmembrane transport / Cell-extracellular matrix interactions / early endosome to late endosome transport / apical dendrite / Fc-gamma receptor I complex binding / cell-cell junction organization / positive regulation of neural precursor cell proliferation / positive regulation of platelet activation / protein localization to cell surface / wound healing, spreading of cells / negative regulation of transcription by RNA polymerase I / megakaryocyte development / GP1b-IX-V activation signalling / cortical cytoskeleton / positive regulation of axon regeneration / receptor clustering / SMAD binding / RHO GTPases activate PAKs / actin filament bundle / brush border / semaphorin-plexin signaling pathway / mitotic spindle assembly / cilium assembly / potassium channel regulator activity / epithelial to mesenchymal transition / blood vessel remodeling / axonal growth cone / heart morphogenesis / positive regulation of substrate adhesion-dependent cell spreading / release of sequestered calcium ion into cytosol / regulation of cell migration / dendritic shaft / protein localization to plasma membrane / G protein-coupled receptor binding / actin filament / protein kinase C binding / synapse organization / mRNA transcription by RNA polymerase II / establishment of protein localization / trans-Golgi network / negative regulation of protein catabolic process / negative regulation of DNA-binding transcription factor activity / cerebral cortex development / small GTPase binding / kinase binding / platelet aggregation / Z disc / positive regulation of protein import into nucleus / cell-cell junction / actin filament binding / actin cytoskeleton / Platelet degranulation / GTPase binding / negative regulation of neuron projection development / actin cytoskeleton organization / postsynapse / perikaryon / angiogenesis / DNA-binding transcription factor binding / positive regulation of canonical NF-kappaB signal transduction / transmembrane transporter binding / protein stabilization / cadherin binding / focal adhesion / glutamatergic synapse / nucleolus / negative regulation of apoptotic process / perinuclear region of cytoplasm / protein homodimerization activity / RNA binding / extracellular exosome / extracellular region / membrane / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Filamin family / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain ...Filamin family / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Immunoglobulin E-set / Immunoglobulin-like fold
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationJournal: Structure / Year: 2019
Title: Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.
Authors: Tatu J K Haataja / Rafael C Bernardi / Simon Lecointe / Romain Capoulade / Jean Merot / Ulla Pentikäinen /
Abstract: Filamin A (FLNa), expressed in endocardial endothelia during fetal valve morphogenesis, is key in cardiac development. Missense mutations in FLNa cause non-syndromic mitral valve dysplasia (FLNA-MVD). ...Filamin A (FLNa), expressed in endocardial endothelia during fetal valve morphogenesis, is key in cardiac development. Missense mutations in FLNa cause non-syndromic mitral valve dysplasia (FLNA-MVD). Here, we aimed to reveal the currently unknown underlying molecular mechanism behind FLNA-MVD caused by the FLNa P637Q mutation. The solved crystal structure of the FLNa3-5 P637Q revealed that this mutation causes only minor structural changes close to mutation site. These changes were observed to significantly affect FLNa's ability to transmit cellular force and to interact with its binding partner. The performed steered molecular dynamics simulations showed that significantly lower forces are needed to split domains 4 and 5 in FLNA-MVD than with wild-type FLNa. The P637Q mutation was also observed to interfere with FLNa's interactions with the protein tyrosine phosphatase PTPN12. Our results provide a crucial step toward understanding the molecular bases behind FLNA-MVD, which is critical for the development of drug-based therapeutics.
Contact author
  • Tatu Haataja (University of Jyväskylä, Jyväskylän, Finland)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #2606
Type: atomic / Chi-square value: 1.001
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Filamin A Ig-like domains 3-5 (FLNa3-5) / Specimen concentration: 1.00-4.00
BufferName: 20 mM Tris, 100 mM NaCl, 1 mM DTT / pH: 8
Entity #851Name: FLNa3-5 / Type: protein / Description: Filamin A Ig-like domains 3-5 / Formula weight: 30.76 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P21333
Sequence: CNPSACRAVG RGLQPKGVRV KETADFKVYT KGAGSGELKV TVKGPKGEER VKQKDLGDGV YGFEYYPMVP GTYIVTITWG GQNIGRSPFE VKVGTECGNQ KVRAWGPGLE GGVVGKSADF VVEAIGDDVG TLGFSVEGPS QAKIECDDKG DGSCDVRYWP QEAGEYAVHV ...Sequence:
CNPSACRAVG RGLQPKGVRV KETADFKVYT KGAGSGELKV TVKGPKGEER VKQKDLGDGV YGFEYYPMVP GTYIVTITWG GQNIGRSPFE VKVGTECGNQ KVRAWGPGLE GGVVGKSADF VVEAIGDDVG TLGFSVEGPS QAKIECDDKG DGSCDVRYWP QEAGEYAVHV LCNSEDIRLS PFMADIRDAP QDFHPDRVKA RGPGLEKTGV AVNKPAEFTV DAKHGGKAPL RVQVQDNEGC PVEALVKDNG NGTYSCSYVP RKPVKHTAMV SWGGVSIPNS PFRVNVGAG

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 2.9 mm
DetectorName: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm
Scan
Title: Filamin A Ig-like domains 3-5 (FLNa3-5) / Measurement date: Feb 10, 2017 / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
MinMax
Q0.06 4.937
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 366 /
MinMax
Q0.07648 3.513
P(R) point4 369
R0 7.34
Result
Type of curve: merged
Comments: SAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated fragment (SASDEP7).
ExperimentalPorod
MW24.7 kDa-
Volume-39 nm3

P(R)GuinierGuinier error
Forward scattering, I025.64 25.64 0.1
Radius of gyration, Rg2.2 nm2.19 nm0.1

MinMaxError
D-7.34 0.5
Guinier point8 114 -

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