SASDAH8: Human Filamin A Ig-like domains 20-21* truncation (2141-2329)

Basic information

• Entry: Database: SASBDB / ID: SASDAH8

Sample

Human Filamin A Ig-like domains 20-21* truncation (2141-2329)

• Human Filamin A Ig-like domains 20-21* (protein), FilaminA*, Homo sapiens

Function / homology

Function:

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 / formation of radial glial scaffolds / glycoprotein Ib-IX-V complex / adenylate cyclase-inhibiting dopamine receptor signaling pathway / 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 / positive regulation of neural precursor cell proliferation / cell-cell junction organization / positive regulation of platelet activation / protein localization to cell surface / Fc-gamma receptor I complex binding / negative regulation of transcription by RNA polymerase I / wound healing, spreading of cells / 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 / cilium assembly / mitotic spindle 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 / regulation of cell migration / release of sequestered calcium ion into cytosol / dendritic shaft / protein kinase C binding / protein localization to plasma membrane / G protein-coupled receptor binding / actin filament / synapse organization / mRNA transcription by RNA polymerase II / trans-Golgi network / establishment of protein localization / negative regulation of DNA-binding transcription factor activity / negative regulation of protein catabolic process / cerebral cortex development / Z disc / small GTPase binding / platelet aggregation / kinase binding / positive regulation of protein import into nucleus / actin filament binding / cell-cell junction / actin cytoskeleton / Platelet degranulation / negative regulation of neuron projection development / GTPase binding / perikaryon / actin cytoskeleton organization / postsynapse / angiogenesis / positive regulation of canonical NF-kappaB signal transduction / DNA-binding transcription factor binding / 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 / cytosol / cytoplasm

Domain/homology:

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

Component:

Filamin-A

• Biological species: Homo sapiens (human)
• Citation: Journal: PLoS One / Year: 2015; Title: Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21.; Authors: Jonne Seppälä / Helena Tossavainen / Nebojsa Rodic / Perttu Permi / Ulla Pentikäinen / Jari Ylänne / ; Abstract: Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds for signaling proteins, and binding several other cytoskeletal proteins that regulate cell adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated that myosin-mediated contractile forces can reveal hidden protein binding sites in the domain pairs IgFLNa18-19 and 20-21, enabling FLNs to transduce mechanical signals in cells. The atomic structures of these mechanosensor domain pairs in the resting state are known, as well as the structures of individual IgFLN21 with ligand peptides. However, little experimental data is available on how interacting protein binding deforms the domain pair structures. Here, using small-angle x-ray scattering-based modelling, x-ray crystallography, and NMR, we show that the adaptor protein migfilin-derived peptide-bound structure of IgFLNa20-21 is flexible and adopts distinctive conformations depending on the presence or absence of the interacting peptide. The conformational changes reported here may be common for all peptides and may play a role in the mechanosensor function of the site.

Contact author

• Jonne Seppälä (University of Jyväskylä)

Models

• Model #321: ; Type: dummy / Software: DAMMIF (r4556) / Radius of dummy atoms: 1.40 A / Chi-square value: 0.752 / P-value: 0.249000; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Human Filamin A Ig-like domains 20-21* truncation (2141-2329); Specimen concentration: 1.00-4.00
• Buffer: Name: Tris / Concentration: 20.00 mM / pH: 8 / Composition: 50 mM NaCl, 10mM DTT

Entity #190

Name: FilaminA* / Type: protein / Description: Human Filamin A Ig-like domains 20-21* / Formula weight: 20 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P21333
Sequence:

KESITRRRRA PSVANVGSHC DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGTH TVSVKYKGQH VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEAGVPAEFS IWTREAGAGG LAIAVEGPSK AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPS

Experimental information

• Beam: Instrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.93 Å / Dist. spec. to detc.: 2.43 mm
• Detector: Name: Pilatus 1M

Scan

Title: Human Filamin A Ig-like domains 20-21* / Measurement date: Feb 1, 2014 / Storage temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /

	Min	Max
Q	0.0937	4.63

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 416 /

	Min	Max
Q	0.209	2.2
P(R) point	25	440
R	0	6.8

Result

Type of curve: merged
Comments: Filamin A fragment residues 2141-2329 (Ig-like domains).

	Experimental	Porod
MW	30 kDa	19 kDa
Volume	-	32 nm3

	P(R)	P(R) error	Guinier
Forward scattering, I0	30	0.038	29.9
Radius of gyration, Rg	1.97 nm	-	1.9 nm

	Min	Max
D	-	6.8
Guinier point	25	110