1XOD
Crystal structure of X. tropicalis Spred1 EVH-1 domain
1XOD の概要
| エントリーDOI | 10.2210/pdb1xod/pdb |
| 分子名称 | Spred1, GLYCEROL (3 entities in total) |
| 機能のキーワード | spred, sprouty, evh1, peptide-binding, signaling protein |
| 由来する生物種 | Xenopus tropicalis (western clawed frog) |
| 細胞内の位置 | Membrane; Peripheral membrane protein (By similarity): Q66JG9 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 26033.17 |
| 構造登録者 | Harmer, N.J.,Sivak, J.M.,Amaya, E.,Blundell, T.L. (登録日: 2004-10-06, 公開日: 2005-01-25, 最終更新日: 2023-08-23) |
| 主引用文献 | Harmer, N.J.,Sivak, J.M.,Amaya, E.,Blundell, T.L. 1.15A Crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family Febs Lett., 579:1161-1166, 2005 Cited by PubMed Abstract: The recently described Spred protein family has been implicated in the modulation of receptor tyrosine kinase signalling. We report the crystal structure of the Enabled/vasodilator-stimulated phosphoprotein homology-1 (EVH1) domain from Xenopus tropicalis Spred1, solved to 1.15 A resolution. This structure confirms that the Spred EVH1 adopts the pleckstrin-homology fold, with a similar secondary structure to Enabled. A translation of one of the peptide-binding groove beta-strands narrows this groove, whilst one end of the groove shows structural flexibility. We propose that Spred1 will bind peptides that are less proline-rich than other EVH1 domains, with conformational changes indicating an induced fit. PubMed: 15710406DOI: 10.1016/j.febslet.2004.11.114 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.15 Å) |
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