Search results for "filamin A"

showing 5 items of 5 documents

Determination of a conformational change in filamin A with Förster resonance energy transfer

2011

Filamins are large rod-like proteins that cross-link actin filaments into three-dimensional networks. They also bind to a plethora of proteins with distinct functions showing that they have a versatile role in cells. Functional filamins are dimers consisting of an N-terminal actin binding domain followed by 24 immunoglobulin-like domains. The most C-terminal domains mediate the dimerization. Two hinge regions are located between the domains 15 and 16 and 23 and 24, respectively, and produce structural flexibility that is essential for the protein function. The domains 18-19 and 20-21 are folded in a pairwise manner in which the first β strands of the even numbered domains are folded along w…

EGFPFRETfilamin Aproteiinit
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Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A

2018

International audience; 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 signi…

Filamins[SDV]Life Sciences [q-bio]Protein Tyrosine Phosphatase Non-Receptor Type 12Heart Valve DiseasesMutation MissenseMorphogenesisProtein tyrosine phosphataseMolecular Dynamics SimulationBiologyFilaminta3111ArticleFLNA-MVD03 medical and health sciencessteered molecular dynamics simulationsStructural Biologymechanical forcesmedicineHumansMitral valve prolapseMissense mutationFLNAmolekyylidynamiikkasydäntauditCell adhesionMolecular Biology030304 developmental biologyX-ray crystallography0303 health sciencesBinding Sites030302 biochemistry & molecular biologyta1182filamiinitprotein tyrosine phosphatase 12medicine.disease3. Good healthCell biologyFilamin AMutation (genetic algorithm)cardiovascular systemMitral Valveproteiinitmitral valve prolapseröntgenkristallografiaProtein Binding
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Congenital emphysematous lung disease associated with a novel Filamin A mutation. Case report and literature review

2019

Abstract Background Progressive lung involvement in Filamin A (FLNA)-related cerebral periventricular nodular heterotopia (PVNH) has been reported in a limited number of cases. Case presentation We report a new pathogenic FLNA gene variant (c.7391_7403del; p.Val2464Alafs*5) in a male infant who developed progressive lung disease with emphysematous lesions and interstitial involvement. Following lobar resection, chronic respiratory failure ensued necessitating continuous mechanical ventilation and tracheostomy. Cerebral periventricular nodular heterotopia was also present. Conclusions We report a novel variant of the FLNA gene, associated with a severe lung disorder and PNVH. The lung disord…

Lung DiseasesMalePathologymedicine.medical_specialtyFilaminsmedicine.medical_treatmentChildren; Congenital enphysema; Filamin a; Lung disease; Periventricular nodular heterotopiaCase ReportFilaminKeywords: Filamin a Congenital enphysema Lung disease Children Periventricular nodular heterotopiaFilamin aLung Disorder03 medical and health sciences0302 clinical medicineNeuroimagingLoss of Function Mutation030225 pediatricsmedicineHumansFLNA030212 general & internal medicineLungChildrenCongenital enphysemaGenetic testingMechanical ventilationLungmedicine.diagnostic_testbusiness.industrylcsh:RJ1-570BrainInfantlcsh:Pediatricsrespiratory systemRespiration ArtificialPeriventricular nodular heterotopiamedicine.anatomical_structurePulmonary EmphysemaRespiratory failureLung diseasePediatrics Perinatology and Child HealthRadiography ThoracicRespiratory InsufficiencyTomography X-Ray ComputedbusinessBMC Pediatrics
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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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Three proteins regulating integrin function - filamin, 14-3-3 and RIAM

2011

integriinitfosforylaatiointegrinphosphorylationRIAMtalinfilamiinitsäätelyproteiinitcytoplasmic interactionsfilamin A variant-1
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