Access
To read this story in full you will need to login or make a payment (see right).
Article
Nature 432, 872-877 (16 December 2004) | doi:10.1038/nature03144; Received 30 September 2004; Accepted 1 November 2004
Open Innovation Challenges
-
Efficient Chromosome Doubling: Plant Cell Division
The Seeker is looking for an efficient chromosome doubling method in plants and in particular, metho...
-
Protect Enzyme from In Planta Degradation
A proposal for stable expression of an enzyme in corn seed is desired.
nature jobs
Postdoctoral Research Fellow positions - Brain and Cognitive Sciences
- Seoul National University
- Seoul Korea
Postdoctoral Fellowship
- Lovelace Respiratory Research Institute
- Albuquerque, New Mexico
Structural basis for the assembly of a nuclear export complex
Yoshiyuki Matsuura & Murray Stewart
- MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
Correspondence to: Murray Stewart Email: ms@mrc-lmb.cam.ac.uk
Atomic coordinates and structure factors have been deposited in the Protein Data Bank under accession codes 1WA5 and rlwa5sf.ent, respectively.
Abstract
The nuclear import and export of macromolecular cargoes through nuclear pore complexes is mediated primarily by carriers such as importin-
. Importins carry cargoes into the nucleus, whereas exportins carry cargoes to the cytoplasm. Transport is orchestrated by nuclear RanGTP, which dissociates cargoes from importins, but conversely is required for cargo binding to exportins. Here we present the 2.0 Å crystal structure of the nuclear export complex formed by exportin Cse1p complexed with its cargo (Kap60p) and RanGTP, thereby providing a structural framework for understanding nuclear protein export and the different functions of RanGTP in export and import. In the complex, Cse1p coils around both RanGTP and Kap60p, stabilizing the RanGTP-state and clamping the Kap60p importin-
-binding domain, ensuring that only cargo-free Kap60p is exported. Mutagenesis indicated that conformational changes in exportins couple cargo binding to high affinity for RanGTP, generating a spring-loaded molecule to facilitate disassembly of the export complex following GTP hydrolysis in the cytoplasm.
- MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
Correspondence to: Murray Stewart Email: ms@mrc-lmb.cam.ac.uk
Atomic coordinates and structure factors have been deposited in the Protein Data Bank under accession codes 1WA5 and rlwa5sf.ent, respectively.
To read this story in full you will need to login or make a payment (see right).
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Nuclear transport HEATs upNature Cell Biology News and Views (01 Jul 1999)
Nuclear transport comes full circleNature Structural & Molecular Biology News and Views (01 May 2009)
See all 11 matches for News And ViewsRESEARCH
A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobinNature Structural Biology Article (01 Jan 1997)
Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38Nature Structural Biology Article (01 Nov 1996)
See all 61 matches for Research
