1F6F
CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN OVINE PLACENTAL LACTOGEN AND THE EXTRACELLULAR DOMAIN OF THE RAT PROLACTIN RECEPTOR
1F6F の概要
| エントリーDOI | 10.2210/pdb1f6f/pdb |
| 分子名称 | PLACENTAL LACTOGEN, PROLACTIN RECEPTOR (3 entities in total) |
| 機能のキーワード | 4-helical bundle, alpha helical bundle, ternary complex, fn iii domains, beta sheet domains, cytokine-receptor complex, hormone-growth factor-hormone receptor complex, hormone/growth factor/hormone receptor |
| 由来する生物種 | Ovis aries (sheep) 詳細 |
| 細胞内の位置 | Secreted: P16038 Membrane; Single-pass type I membrane protein: P05710 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 71770.63 |
| 構造登録者 | Elkins, P.A.,Christinger, H.W.,Sandowski, Y.,Sakal, E.,Gertler, A.,De Vos, A.M.,Kossiakoff, A.A. (登録日: 2000-06-21, 公開日: 2000-07-04, 最終更新日: 2024-10-30) |
| 主引用文献 | Elkins, P.A.,Christinger, H.W.,Sandowski, Y.,Sakal, E.,Gertler, A.,de Vos, A.M.,Kossiakoff, A.A. Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor. Nat.Struct.Biol., 7:808-815, 2000 Cited by PubMed Abstract: The structure of the ternary complex between ovine placental lactogen (oPL) and the extracellular domain (ECD) of the rat prolactin receptor (rPRLR) reveals that two rPRLR ECDs bind to opposite sides of oPL with pseudo two-fold symmetry. The two oPL receptor binding sites differ significantly in their topography and electrostatic character. These binding interfaces also involve different hydrogen bonding and hydrophobic packing patterns compared to the structurally related human growth hormone (hGH)-receptor complexes. Additionally, the receptor-receptor interactions are different from those of the hGH-receptor complex. The conformational adaptability of prolactin and growth hormone receptors is evidenced by the changes in local conformations of the receptor binding loops and more global changes induced by shifts in the angular relationships between the N- and C-terminal domains, which allow the receptor to bind to the two topographically distinct sites of oPL. PubMed: 10966654DOI: 10.1038/79047 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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