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PDBsum entry 5dis
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Transport protein
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PDB id
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5dis
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Contents |
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1032 a.a.
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172 a.a.
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264 a.a.
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395 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural and functional characterization of crm1-Nup214 interactions reveals multiple fg-Binding sites involved in nuclear export.
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Authors
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S.A.Port,
T.Monecke,
A.Dickmanns,
C.Spillner,
R.Hofele,
H.Urlaub,
R.Ficner,
R.H.Kehlenbach.
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Ref.
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Cell Rep, 2015,
13,
690-702.
[DOI no: ]
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PubMed id
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Abstract
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CRM1 is the major nuclear export receptor. During translocation through the
nuclear pore, transport complexes transiently interact with
phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic
side of the nuclear pore, CRM1 tightly interacts with the nucleoporin Nup214.
Here, we present the crystal structure of a 117-amino-acid FG-repeat-containing
fragment of Nup214, in complex with CRM1, Snurportin 1, and RanGTP at 2.85 Å
resolution. The structure reveals eight binding sites for Nup214 FG motifs on
CRM1, with intervening stretches that are loosely attached to the transport
receptor. Nup214 binds to N- and C-terminal regions of CRM1, thereby clamping
CRM1 in a closed conformation and stabilizing the export complex. The role of
conserved hydrophobic pockets for the recognition of FG motifs was analyzed in
biochemical and cell-based assays. Comparative studies with RanBP3 and Nup62
shed light on specificities of CRM1-nucleoporin binding, which serves as a
paradigm for transport receptor-nucleoporin interactions.
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Secondary reference #1
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Title
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Combining dehydration, Construct optimization and imp data collection to solve the crystal structure of a crm1-Rangtp-Spn1-Nup214 quaternary export complex
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Authors
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T.Monecke,
A.Dickmanns,
M.S.Weiss,
S.A.Port,
R.H.Kehlenbar.Ficner.
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Ref.
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TO BE PUBLISHED ...
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