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

基本情報

• 登録情報: データベース: SASBDB / ID: SASDAH8

試料

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

• Human Filamin A Ig-like domains 20-21* (protein), FilaminA*, 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 / blood coagulation, intrinsic pathway / tubulin deacetylation / OAS antiviral response / actin crosslink formation / positive regulation of actin filament bundle assembly / positive regulation of neuron migration / protein localization to bicellular tight junction / Cell-extracellular matrix interactions / positive regulation of potassium ion transmembrane transport / positive regulation of platelet activation / apical dendrite / positive regulation of neural precursor cell proliferation / Fc-gamma receptor I complex binding / podosome / 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 / SMAD binding / receptor clustering / cortical cytoskeleton / semaphorin-plexin signaling pathway / RHO GTPases activate PAKs / cilium assembly / : / mitotic spindle assembly / potassium channel regulator activity / release of sequestered calcium ion into cytosol / positive regulation of substrate adhesion-dependent cell spreading / regulation of cell migration / dendritic shaft / protein localization to plasma membrane / actin filament / establishment of protein localization / protein sequestering activity / negative regulation of protein catabolic process / cerebral cortex development / positive regulation of protein import into nucleus / G protein-coupled receptor binding / mRNA transcription by RNA polymerase II / platelet aggregation / Z disc / small GTPase binding / kinase binding / cell-cell junction / actin filament binding / Platelet degranulation / actin cytoskeleton / growth cone / actin cytoskeleton organization / GTPase binding / DNA-binding transcription factor binding / perikaryon / 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 / membrane / nucleus / plasma membrane / cytoplasm / cytosol

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

• モデル #321: ; タイプ: dummy / ソフトウェア: DAMMIF (r4556) / ダミー原子の半径: 1.40 A / カイ2乗値: 0.752 / P-value: 0.249000; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Human Filamin A Ig-like domains 20-21* truncation (2141-2329); 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 #190

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

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

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 Ig-like domains 20-21* / 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	0.0937	4.63

距離分布関数 P(R)

ソフトウェア P(R): GNOM 4.6 / ポイント数: 416 /

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

結果

カーブのタイプ: merged
コメント: Filamin A fragment residues 2141-2329 (Ig-like domains).

	実験値	Porod
分子量	30 kDa	19 kDa
体積	-	32 nm3

	P(R)	P(R) error	Guinier
前方散乱 I0	30	0.038	29.9
慣性半径, Rg	1.97 nm	-	1.9 nm

	Min	Max
D	-	6.8
Guinier point	25	110