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Article

Structural basis for substrate recognition and dissociation by human transportin 1.

Molecular cell - 12 Oct 2007

Imasaki Tsuyoshi, Shimizu Toshiyuki, Hashimoto Hiroshi, Hidaka Yuji, Kose Shingo, Imamoto Naoko, Yamada Michiyuki, Sato Mamoru

Abstract excerpt

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...

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Share to Active Transport, Cell Nucleus
Share to ATP Binding Cassette Transporter, Subfamily B, Member 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 17936704
DOI: 10.1016/j.molcel.2007.08.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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