1XFE
Solution structure of the LA7-EGFA pair from the LDL receptor
1XFE の概要
| エントリーDOI | 10.2210/pdb1xfe/pdb |
| 分子名称 | Low-density lipoprotein receptor, CALCIUM ION (2 entities in total) |
| 機能のキーワード | ligand-binding repeat, egf-like repeat, lipid transport, endocytosis-exocytosis complex, endocytosis/exocytosis |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cell membrane; Single-pass type I membrane protein: P01130 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 9295.57 |
| 構造登録者 | Beglova, N.,Jeon, H.,Fisher, C.,Blacklow, S.C. (登録日: 2004-09-14, 公開日: 2004-11-02, 最終更新日: 2024-10-30) |
| 主引用文献 | Beglova, N.,Jeon, H.,Fisher, C.,Blacklow, S.C. Cooperation between Fixed and Low pH-Inducible Interfaces Controls Lipoprotein Release by the LDL Receptor Mol.Cell, 16:281-292, 2004 Cited by PubMed Abstract: Low-density lipoprotein (LDL) receptors bind lipoprotein particles at the cell surface and release them in the low pH environment of the endosome. The published structure of the receptor determined at endosomal pH reveals an interdomain interface between its beta propeller and its fourth and fifth ligand binding (LA) repeats, suggesting that the receptor adopts a closed conformation at low pH to release LDL. Here, we combine lipoprotein binding and release assays with NMR spectroscopy to examine structural features of the receptor promoting release of LDL at low pH. These studies lead to a model in which the receptor uses a pH-invariant scaffold as an anchor to restrict conformational search space, combining it with flexible linkers between ligand binding repeats to interconvert between open and closed conformations. This finely tuned balance between interdomain rigidity and flexibility is likely to represent a shared structural feature in proteins of the LDL receptor family. PubMed: 15494314DOI: 10.1016/j.molcel.2004.09.038 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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