Search results for "FLNA"

showing 4 items of 14 documents

The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended

2012

Filamins are large proteins that cross-link actin filaments and connect to other cellular components. The C-terminal rod 2 region of FLNa (filamin A) mediates dimerization and interacts with several transmembrane receptors and intracellular signalling adaptors. SAXS (small-angle X-ray scattering) experiments were used to make a model of a six immunoglobulin-like domain fragment of the FLNa rod 2 (domains 16–21). This fragment had a surprising three-branched structural arrangement, where each branch was made of a tightly packed two-domain pair. Peptides derived from transmembrane receptors and intracellular signalling proteins induced a more open structure of the six domain fragment. Mutagen…

Models Moleculargenetics [Receptors Dopamine D3]metabolism [Recombinant Proteins]Protein Conformationgenetics [Antigens CD18]chemistry [Recombinant Proteins]Plasma protein bindingCrystallography X-RayLigandsFilaminmetabolism [Antigens CD18]metabolism [Cytoskeletal Proteins]BiochemistryfilaminsContractile ProteinsProtein structuremetabolism [Peptide Fragments]FLNAchemistry [Antigens CD18]genetics [Cell Adhesion Molecules]Small-angle X-ray scatteringMicrofilament Proteinsgenetics [Contractile Proteins]Recombinant Proteinschemistry [Receptors Dopamine D3]FBLIM1 protein humanddc:540Domain (ring theory)DimerizationProtein Bindingchemistry [Contractile Proteins]FilaminsAntigens CD18metabolism [Cell Adhesion Molecules]BiologyScattering Small Anglemetabolism [Receptors Dopamine D3]Humanschemistry [Microfilament Proteins]Protein Interaction Domains and Motifsmetabolism [Mutant Proteins]DRD3 protein humanMolecular Biologymetabolism [Contractile Proteins]Actingenetics [Cytoskeletal Proteins]Cryoelectron MicroscopyMutagenesista1182Receptors Dopamine D3metabolism [Microfilament Proteins]Cell Biologychemistry [Cell Adhesion Molecules]genetics [Peptide Fragments]Peptide FragmentsCytoskeletal ProteinsCrystallographychemistry [Mutant Proteins]chemistry [Peptide Fragments]CD18 AntigensBiophysicschemistry [Cytoskeletal Proteins]Mutant Proteinsgenetics [Microfilament Proteins]Cell Adhesion MoleculesBiochemical Journal
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Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia

2019

Mitral valve diseases affect approximately 3% of the population and are the most common reasons for valvular surgery because no drug-based treatments exist. Inheritable genetic mutations have now been established as the cause of mitral valve insufficiency, and four different missense mutations in the filamin A gene (FLNA) have been found in patients suffering from non-syndromic mitral valve dysplasia (MVD). The FLNA protein is expressed, in particular, in endocardial endothelia during fetal valve morphogenesis and is key in cardiac development. The FLNA-MVD causing mutations are clustered in the N-terminal region of FLNA. How the mutations in FLNA modify its structure and function, have mos…

Protein FoldingdysplasiatFilamins[SDV]Life Sciences [q-bio]PopulationProtein Tyrosine Phosphatase Non-Receptor Type 12BiophysicsMutation Missensesynnynnäiset sydänviatProtein tyrosine phosphataseBiologyMolecular Dynamics Simulationmedicine.disease_causeFilamin03 medical and health sciences0302 clinical medicinemitral valve dysplasiaMitral valvemedicineFLNAMissense mutationHumanseducationGene030304 developmental biologyGenetics0303 health sciencesMutationeducation.field_of_studyBinding SitesMitral Valve Prolapsecritical structural defectshiippaläppäfilamiinitArticles3. Good healthmedicine.anatomical_structurecardiovascular systemfilamin A mutationsgeneettiset tekijätmutaatiot030217 neurology & neurosurgeryProtein Binding
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Cystic Fibrosis Transmembrane Conductance Regulator Interacts with Multiple Immunoglobulin Domains of Filamin A

2010

Mutations of the chloride channel cystic fibrosis transmembrane conductance regulator (CFTR) that impair its apical localization and function cause cystic fibrosis. A previous report has shown that filamin A (FLNa), an actin-cross-linking and -scaffolding protein, interacts directly with the cytoplasmic N terminus of CFTR and that this interaction is necessary for stability and confinement of the channel to apical membranes. Here, we report that the CFTR N terminus has sequence similarity to known FLNa-binding partner-binding sites. FLNa has 24 Ig (IgFLNa) repeats, and a CFTR peptide pulled down repeats 9, 12, 17, 19, 21, and 23, which share sequence similarity yet differ from the other FLN…

Scaffold proteincongenital hereditary and neonatal diseases and abnormalitiesFilaminsMolecular Sequence DataCystic Fibrosis Transmembrane Conductance RegulatorImmunoglobulinsBiologymedicine.disease_causeFilaminBiochemistryContractile ProteinsProtein structureCricetinaemedicineAnimalsHumansFLNAAmino Acid SequenceMolecular BiologyPeptide sequenceMutationSequence Homology Amino AcidCell MembraneMicrofilament ProteinsCell Biologyrespiratory systemMolecular biologyActinsCystic fibrosis transmembrane conductance regulatorProtein Structure Tertiaryrespiratory tract diseasesCell biologySolubilityMutationProtein Structure and FoldingChloride channelbiology.proteinPeptidesDimerizationProtein BindingJournal of Biological Chemistry
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Effect of ligand-binding on protein function

2014

tietokonesimulointifilamiinitliganditsitoutuminenionotrooppiset glutamaattireseptoritfilaminpeptidiliganditmolecular dynamicsionotropic glutamate receptorlääkesuunnitteluFLNaiGluRlaskennallinen tiedelaskennalliset menetelmätmolekyylidynamiikkaTCPTPsimulointiproteiinitbinding free energyT-cell protein tyrosine phosphatase
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