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基本情報
登録情報 | データベース: SASBDB / ID: SASDAB8 |
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![]() | Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).
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機能・相同性 | ![]() G protein-coupled glutamate receptor binding / membrane curvature sensor activity / postsynaptic early endosome / postsynaptic endocytic zone / glial cell development / cellular response to decreased oxygen levels / Arp2/3 complex binding / postsynaptic specialization / regulation of Arp2/3 complex-mediated actin nucleation / negative regulation of Arp2/3 complex-mediated actin nucleation ...G protein-coupled glutamate receptor binding / membrane curvature sensor activity / postsynaptic early endosome / postsynaptic endocytic zone / glial cell development / cellular response to decreased oxygen levels / Arp2/3 complex binding / postsynaptic specialization / regulation of Arp2/3 complex-mediated actin nucleation / negative regulation of Arp2/3 complex-mediated actin nucleation / SNAP receptor activity / dopamine transport / monoamine transport / : / dendritic spine organization / regulation of postsynaptic neurotransmitter receptor internalization / long-term synaptic depression / dendritic spine maintenance / receptor clustering / Trafficking of GluR2-containing AMPA receptors / regulation of insulin secretion / positive regulation of receptor internalization / protein targeting / cellular response to glucose starvation / cytoskeletal protein binding / ionotropic glutamate receptor binding / ephrin receptor binding / trans-Golgi network membrane / G protein-coupled receptor binding / protein kinase C binding / intracellular protein transport / phospholipid binding / receptor tyrosine kinase binding / actin filament binding / synaptic vesicle / GTPase binding / presynaptic membrane / dendritic spine / postsynaptic density / cytoskeleton / neuron projection / protein domain specific binding / protein phosphorylation / negative regulation of gene expression / signaling receptor binding / glutamatergic synapse / synapse / dendrite / perinuclear region of cytoplasm / Golgi apparatus / protein-containing complex / mitochondrion / identical protein binding / metal ion binding / plasma membrane / cytoplasm 類似検索 - 分子機能 |
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![]() | ![]() タイトル: Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering. 著者: Morten L Karlsen / Thor S Thorsen / Niklaus Johner / Ina Ammendrup-Johnsen / Simon Erlendsson / Xinsheng Tian / Jens B Simonsen / Rasmus Høiberg-Nielsen / Nikolaj M Christensen / George ...著者: Morten L Karlsen / Thor S Thorsen / Niklaus Johner / Ina Ammendrup-Johnsen / Simon Erlendsson / Xinsheng Tian / Jens B Simonsen / Rasmus Høiberg-Nielsen / Nikolaj M Christensen / George Khelashvili / Werner Streicher / Kaare Teilum / Bente Vestergaard / Harel Weinstein / Ulrik Gether / Lise Arleth / Kenneth L Madsen / ![]() ![]() 要旨: PICK1 is a neuronal scaffolding protein containing a PDZ domain and an auto-inhibited BAR domain. BAR domains are membrane-sculpting protein modules generating membrane curvature and promoting ...PICK1 is a neuronal scaffolding protein containing a PDZ domain and an auto-inhibited BAR domain. BAR domains are membrane-sculpting protein modules generating membrane curvature and promoting membrane fission. Previous data suggest that BAR domains are organized in lattice-like arrangements when stabilizing membranes but little is known about structural organization of BAR domains in solution. Through a small-angle X-ray scattering (SAXS) analysis, we determine the structure of dimeric and tetrameric complexes of PICK1 in solution. SAXS and biochemical data reveal a strong propensity of PICK1 to form higher-order structures, and SAXS analysis suggests an offset, parallel mode of BAR-BAR oligomerization. Furthermore, unlike accessory domains in other BAR domain proteins, the positioning of the PDZ domains is flexible, enabling PICK1 to perform long-range, dynamic scaffolding of membrane-associated proteins. Together with functional data, these structural findings are compatible with a model in which oligomerization governs auto-inhibition of BAR domain function. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
-モデル
モデル #318 | ![]() タイプ: mix / ソフトウェア: EOM / ダミー原子の半径: 1.90 A / カイ2乗値: 3.818116 ![]() |
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モデル #319 | ![]() タイプ: mix / ソフトウェア: EOM / ダミー原子の半径: 1.90 A / カイ2乗値: 3.818116 ![]() |
モデル #322 | ![]() タイプ: mix / ソフトウェア: EOM / ダミー原子の半径: 1.90 A / カイ2乗値: 3.818116 ![]() |
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試料
![]() | 名称: Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition). 試料濃度: 4.20-8.80 |
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バッファ | 名称: 50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100 / 濃度: 50.00 mM / pH: 7.4 / 組成: 125 mM NaCl, 0.01 vol% reduced TX-100 |
要素 #184 | タイプ: protein / 記述: PRKCA-binding protein / 分子量: 46.506 / 分子数: 2 / 由来: Rattus norvegicus / 参照: UniProt: Q9EP80 配列: MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT ...配列: MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSGN YEYRLILRCR QEARARFSQM RKDVLEKMEL LDQKHVQDIV FQLQRLVSTM SKYYNDCYAV LRDADVFPIE VDLAHTTLAY GPNQGGFTDG EDEEEEEEDG AAREVSKDAR GATGPTDKGG SWLKV |
-実験情報
ビーム | 設備名称: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||
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検出器 | 名称: MAR 345 Image Plate | ||||||||||||||||||||||||||||||||||||
スキャン | 測定日: 2015年5月11日 / セル温度: 4 °C / 照射時間: 40 sec. / フレーム数: 4 / 単位: 1/nm /
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距離分布関数 P(R) |
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結果 | コメント: Structure and flexibility of PICK1 LKV mutant dimer was characterized by SAXS using data obtained by decomposing scattering from two polydisperse samples into dimer (and tetramer) ...コメント: Structure and flexibility of PICK1 LKV mutant dimer was characterized by SAXS using data obtained by decomposing scattering from two polydisperse samples into dimer (and tetramer) contributions. To obtain the dimer scattering, two samples were measured at 4.4 and 8,8 mg/ml, and decomposed as described in the reference. Models were fitted to data using a combination of rigid body modelling and EOM, based on structural components defined by NMR and MD simulations. PDB files represent structures found in the optimal ensemble. All data, in addition to that displayed for this entry, are available in the .zip archive.
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