2Z5M
Complex of Transportin 1 with TAP NLS, crystal form 2
2Z5M の概要
エントリーDOI | 10.2210/pdb2z5m/pdb |
関連するPDBエントリー | 1qbk 2Z5J 2Z5K 2Z5N 2Z5O 2h4m 2ot8 |
分子名称 | Transportin-1, Nuclear RNA export factor 1 (2 entities in total) |
機能のキーワード | nuclear transport, importin, exportin, karyopherin, nucleocytoplasmic, tap, nls, transport protein-rna binding protein complex, transport protein/rna binding protein |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Cytoplasm: Q92973 Nucleus, nucleoplasm : Q9UBU9 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 104895.12 |
構造登録者 | Imasaki, T.,Shimizu, T.,Hashimoto, H.,Hidaka, Y.,Kose, S.,Imamoto, N.,Yamada, M.,Sato, M. (登録日: 2007-07-14, 公開日: 2007-10-23, 最終更新日: 2023-11-01) |
主引用文献 | Imasaki, T.,Shimizu, T.,Hashimoto, H.,Hidaka, Y.,Kose, S.,Imamoto, N.,Yamada, M.,Sato, M. Structural basis for substrate recognition and dissociation by human transportin 1 Mol.Cell, 28:57-67, 2007 Cited by PubMed Abstract: Transportin 1 (Trn1) is a transport receptor that transports substrates from the cytoplasm to the nucleus through nuclear pore complexes by recognizing nuclear localization signals (NLSs). Here we describe four crystal structures of human Trn1 in a substrate-free form as well as in the complex with three NLSs (hnRNP D, JKTBP, and TAP, respectively). Our data have revealed that (1) Trn1 has two sites for binding NLSs, one with high affinity (site A) and one with low affinity (site B), and NLS interaction at site B controls overall binding affinity for Trn1; (2) Trn1 recognizes the NLSs at site A followed by conformational change at site B to interact with the NLSs; and (3) a long flexible loop, characteristic of Trn1, interacts with site B, thereby displacing transport substrate in the nucleus. These studies provide deep understanding of substrate recognition and dissociation by Trn1 in import pathways. PubMed: 17936704DOI: 10.1016/j.molcel.2007.08.006 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3 Å) |
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