+
データを開く
-
基本情報
| 登録情報 | データベース: PDB / ID: 1d0r | ||||||
|---|---|---|---|---|---|---|---|
| タイトル | SOLUTION STRUCTURE OF GLUCAGON-LIKE PEPTIDE-1-(7-36)-AMIDE IN TRIFLUOROETHANOL/WATER | ||||||
要素 | GLUCAGON-LIKE PEPTIDE-1-(7-36)-AMIDE | ||||||
キーワード | HORMONE/GROWTH FACTOR / SYNTHETIC HORMONE / HORMONE-GROWTH FACTOR COMPLEX | ||||||
| 機能・相同性 | 機能・相同性情報glucagon receptor binding / : / negative regulation of execution phase of apoptosis / feeding behavior / positive regulation of calcium ion import / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of gluconeogenesis / cellular response to glucagon stimulus / regulation of insulin secretion ...glucagon receptor binding / : / negative regulation of execution phase of apoptosis / feeding behavior / positive regulation of calcium ion import / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of gluconeogenesis / cellular response to glucagon stimulus / regulation of insulin secretion / response to activity / gluconeogenesis / hormone activity / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / Glucagon signaling in metabolic regulation / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Glucagon-type ligand receptors / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / glucose homeostasis / secretory granule lumen / G alpha (s) signalling events / G alpha (q) signalling events / positive regulation of ERK1 and ERK2 cascade / G protein-coupled receptor signaling pathway / receptor ligand activity / endoplasmic reticulum lumen / signaling receptor binding / negative regulation of apoptotic process / extracellular space / extracellular region / identical protein binding / plasma membrane 類似検索 - 分子機能 | ||||||
| 生物種 | Homo sapiens (ヒト) | ||||||
| 手法 | 溶液NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
データ登録者 | Chang, X. / Keller, D. / Bjorn, S. / Led, J.J. | ||||||
引用 | ジャーナル: MAGN.RESON.CHEM. / 年: 2001 タイトル: Structure and Folding of Glucagon-like Peptide-1-(7-36)-amide in Trifluoroethanol Studied by NMR 著者: Chang, X. / Keller, D. / Bjorn, S. / Led, J.J. #1: ジャーナル: FEBS Lett. / 年: 2002タイトル: NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer 著者: Chang, X. / Keller, D. / O'Donoghue, S.I. / Led, J.J. | ||||||
| 履歴 |
|
-
構造の表示
| 構造ビューア | 分子: Molmil Jmol/JSmol |
|---|
-
ダウンロードとリンク
-
ダウンロード
| PDBx/mmCIF形式 | 1d0r.cif.gz | 186.4 KB | 表示 | PDBx/mmCIF形式 |
|---|---|---|---|---|
| PDB形式 | pdb1d0r.ent.gz | 151.9 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 1d0r.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| 文書・要旨 | 1d0r_validation.pdf.gz | 352.5 KB | 表示 | wwPDB検証レポート |
|---|---|---|---|---|
| 文書・詳細版 | 1d0r_full_validation.pdf.gz | 450.2 KB | 表示 | |
| XML形式データ | 1d0r_validation.xml.gz | 15.7 KB | 表示 | |
| CIF形式データ | 1d0r_validation.cif.gz | 24 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/d0/1d0r ftp://data.pdbj.org/pub/pdb/validation_reports/d0/1d0r | HTTPS FTP |
-関連構造データ
-
リンク
-
集合体
| 登録構造単位 | ![]()
| |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| 1 |
| |||||||||
| NMR アンサンブル |
|
-
要素
| #1: タンパク質・ペプチド | 分子量: 3302.648 Da / 分子数: 1 / 由来タイプ: 組換発現 / 詳細: RECOMBINANT FORM / 由来: (組換発現) Homo sapiens (ヒト) / 発現宿主: ![]() |
|---|
-実験情報
-実験
| 実験 | 手法: 溶液NMR | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| NMR実験 |
| ||||||||||||||||||||
| NMR実験の詳細 | Text: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR TECHNIQUES. |
-
試料調製
| 詳細 |
| ||||||
|---|---|---|---|---|---|---|---|
| 試料状態 | pH: 2.5 / 圧: AMBIENT / 温度: 300 K | ||||||
| 結晶化 | *PLUS 手法: other / 詳細: NMR |
-NMR測定
| NMRスペクトロメーター |
|
|---|
-
解析
| NMR software |
| ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 精密化 | 手法: DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS ソフトェア番号: 1 詳細: THE STRUCTURES ARE BASED ON 280 NOE-DERIVED DISTANCE CONSTRAINTS, AND 24 DISTANCE RESTRAINTS FROM HYDROGEN BONDS | ||||||||||||
| 代表構造 | 選択基準: lowest energy | ||||||||||||
| NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 40 / 登録したコンフォーマーの数: 20 | ||||||||||||
| NMR ensemble rms | Atom type: all backbone atoms / Bond angle rms dev: 3.3 ° / Chain range begin: A / Chain range end: A Coord average rmsd method: THE AVERAGE OF THE RMSD TO THE MEAN OF THE 20 NMR CONFORMERS AS DESCRIBED IN REFERENCE JRNL IS 2.92 ANGSTROMS FOR THE N, C AND CA BACKBONE ATOMS Covalent bond rms dev: 0.0144 Å / Improper torsion angle rms dev: 0.33 ° / Residue range begin: 1 / Residue range end: 30 |
ムービー
コントローラー
万見について




Homo sapiens (ヒト)
引用







PDBj










X-PLOR