SASDAE8: Human Filamin A Ig-like domains 20-21 truncation (2151-2329) in c...

基本情報

登録情報

データベース: SASBDB / ID: SASDAE8

試料

Human Filamin A Ig-like domains 20-21 truncation (2151-2329) in complex with migfilin peptide

• Human Filamin A Ig-like domains 20-21/migfilin peptide complex (protein), FilaminA/migfilin, Homo sapiens

機能・相同性

分子機能:

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 / actin crosslink formation / blood coagulation, intrinsic pathway / tubulin deacetylation / OAS antiviral response / positive regulation of actin filament bundle assembly / positive regulation of neuron migration / protein localization to bicellular tight junction / Fc-gamma receptor I complex binding / Cell-extracellular matrix interactions / apical dendrite / positive regulation of potassium ion transmembrane transport / positive regulation of neural precursor cell proliferation / positive regulation of platelet activation / protein localization to cell surface / wound healing, spreading of cells / podosome / negative regulation of transcription by RNA polymerase I / megakaryocyte development / GP1b-IX-V activation signalling / SMAD binding / receptor clustering / cortical cytoskeleton / RHO GTPases activate PAKs / semaphorin-plexin signaling pathway / cilium assembly / mitotic spindle assembly / potassium channel regulator activity / negative regulation of DNA-binding transcription factor activity / release of sequestered calcium ion into cytosol / positive regulation of substrate adhesion-dependent cell spreading / protein sequestering activity / regulation of cell migration / dendritic shaft / protein localization to plasma membrane / actin filament / establishment of protein localization / mRNA transcription by RNA polymerase II / G protein-coupled receptor binding / cerebral cortex development / negative regulation of protein catabolic process / positive regulation of protein import into nucleus / small GTPase binding / platelet aggregation / kinase binding / Z disc / actin filament binding / cell-cell junction / Platelet degranulation / actin cytoskeleton / growth cone / GTPase binding / actin cytoskeleton organization / perikaryon / DNA-binding transcription factor binding / transmembrane transporter binding / positive regulation of canonical NF-kappaB signal transduction / postsynapse / protein stabilization / cadherin binding / focal adhesion / negative regulation of apoptotic process / nucleolus / perinuclear region of cytoplasm / glutamatergic synapse / protein homodimerization activity / RNA binding / extracellular exosome / extracellular region / nucleus / membrane / plasma membrane / cytosol / cytoplasm

ドメイン・相同性:

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

構成要素:

Filamin-A

• 生物種: Homo sapiens (ヒト)
• 引用: ジャーナル: PLoS One / 年: 2015; タイトル: Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21.; 著者: Jonne Seppälä / Helena Tossavainen / Nebojsa Rodic / Perttu Permi / Ulla Pentikäinen / Jari Ylänne / ; 要旨: 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.

登録者

• Jonne Seppälä (University of Jyväskylä)

モデル

試料

• 試料: 名称: Human Filamin A Ig-like domains 20-21 truncation (2151-2329) in complex with migfilin peptide; 試料濃度: 1.00-4.00
• バッファ: 名称: Tris / 濃度: 20.00 mM / pH: 8 / 組成: 50 mM NaCl, 10mM DTT

要素 #187

名称: FilaminA/migfilin / タイプ: protein
記述: Human Filamin A Ig-like domains 20-21/migfilin peptide complex
分子量: 21.3 / 分子数: 1 / 由来: Homo sapiens / 参照: UniProt: P21333
配列:

SVANVGSHCD LSLKIPEISI QDMTAQVTSP SGKTHEAEIV EGENHTYCIR FVPAEMGTHT VSVKYKGQHV PGSPFQFTVG PLGEGGAHKV RAGGPGLERA EAGVPAEFSI WTREAGAGGL AIAVEGPSKA EISFEDRKDG SCGVAYVVQE PGDYEVSVKF NEEHIPDSPF VVPVASPS

実験情報

• ビーム: 設備名称: ESRF BM29 / 地域: Grenoble / 国: France / 線源: X-ray synchrotron / 波長: 0.93 Å / スペクトロメータ・検出器間距離: 2.43 mm
• 検出器: 名称: Pilatus 1M

スキャン

タイトル: Human Filamin A domains 20-21/migfilin peptide
測定日: 2014年2月1日 / 保管温度: 20 °C / 照射時間: 1 sec. / フレーム数: 10 / 単位: 1/nm /

	Min	Max
Q	0.103	4.66

距離分布関数 P(R)

ソフトウェア P(R): GNOM 4.6 / ポイント数: 500 /

	Min	Max
Q	0.219	2.62
P(R) point	25	524
R	0	8.16

結果

カーブのタイプ: merged
コメント: Filamin A fragment residues 2151-2329 (Ig-like domains) in complex with migfilin peptide. NOTE: The displayed SAXS data and data used for P(r) vs r determination are on different I(s) scales.

	実験値	Porod
分子量	30 kDa	18.3 kDa
体積	-	31.1 nm3

	P(R)	Guinier
前方散乱 I0	30.1	22.5
慣性半径, Rg	2.5 nm	2.41 nm

	Min	Max
D	-	8.16
Guinier point	27	89