2P01
The structure of receptor-associated protein(RAP)
2P01 の概要
| エントリーDOI | 10.2210/pdb2p01/pdb |
| 関連するPDBエントリー | 2P03 |
| 分子名称 | Alpha-2-macroglobulin receptor-associated protein (1 entity in total) |
| 機能のキーワード | receptor-associated protein, rap, cell adhesion |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Endoplasmic reticulum: P30533 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 37849.60 |
| 構造登録者 | Lee, D.,Walsh, J.D.,Migliorini, M.,Yu, P.,Cai, T.,Schwieters, C.D.,Krueger, S.,Strickland, D.K.,Wang, Y.X. (登録日: 2007-02-28, 公開日: 2007-08-21, 最終更新日: 2024-05-22) |
| 主引用文献 | Lee, D.,Walsh, J.D.,Migliorini, M.,Yu, P.,Cai, T.,Schwieters, C.D.,Krueger, S.,Strickland, D.K.,Wang, Y.X. The structure of receptor-associated protein (RAP). Protein Sci., 16:1628-1640, 2007 Cited by PubMed Abstract: The receptor-associated protein (RAP) is a molecular chaperone that binds tightly to certain newly synthesized LDL receptor family members in the endoplasmic reticulum (ER) and facilitates their delivery to the Golgi. We have adopted a divide-and-conquer strategy to solve the structures of the individual domains of RAP using NMR spectroscopy. We present here the newly determined structure of domain 2. Based on this structure and the structures of domains 1 and 3, which were solved previously, we utilized experimental small-angle neutron scattering (SANS) data and a novel simulated annealing protocol to characterize the overall structure of RAP. The results reveal that RAP adopts a unique structural architecture consisting of three independent three-helix bundles that are connected by long and flexible linkers. The flexible linkers and the quasi-repetitive structural architecture may allow RAP to adopt various possible conformations when interacting with the LDL receptors, which are also made of repetitive substructure units. PubMed: 17656581DOI: 10.1110/ps.072865407 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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