2Z5M

Complex of Transportin 1 with TAP NLS, crystal form 2

Summary for 2Z5M

• Entry DOI: 10.2210/pdb2z5m/pdb
• Related: 1qbk 2Z5J 2Z5K 2Z5N 2Z5O 2h4m 2ot8
• Descriptor: Transportin-1, Nuclear RNA export factor 1 (2 entities in total)
• Functional Keywords: nuclear transport, importin, exportin, karyopherin, nucleocytoplasmic, tap, nls, transport protein-rna binding protein complex, transport protein/rna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q92973; Nucleus, nucleoplasm : Q9UBU9
• Total number of polymer chains: 2
• Total formula weight: 104895.12

Authors

Imasaki, T.,Shimizu, T.,Hashimoto, H.,Hidaka, Y.,Kose, S.,Imamoto, N.,Yamada, M.,Sato, M. (deposition date: 2007-07-14, release date: 2007-10-23, Last modification date: 2023-11-01)

Primary citation

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

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: 17936704
DOI: 10.1016/j.molcel.2007.08.006

Experimental method

X-RAY DIFFRACTION (3 Å)