Structural highlights
Function
[NU153_RAT] Possible DNA-binding subunit of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Nucleoporin (Nup) 153 is a highly mobile, multifunctional, and essential nuclear pore protein. It contains four zinc finger motifs that are thought to be crucial for the regulation of transport-receptor/cargo interactions via their binding to the small guanine nucleotide binding protein, Ran. We found this interaction to be independent of the phoshorylation state of the nucleotide. Ran binds with the highest affinity to the second zinc finger motif of Nup153 (Nup153ZnF2). Here we present the crystal structure of this complex, revealing a new type of Ran-Ran interaction partner interface together with the solution structure of Nup153ZnF2. According to our complex structure, Nup153ZnF2 binding to Ran excludes the formation of a Ran-importin-beta complex. This finding suggests a local Nup153-mediated Ran reservoir at the nucleoplasmic distal ring of the nuclear pore, where nucleotide exchange may take place in a ternary Nup153-Ran-RCC1 complex, so that import complexes are efficiently terminated.
The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex.,Schrader N, Koerner C, Koessmeier K, Bangert JA, Wittinghofer A, Stoll R, Vetter IR Structure. 2008 Jul;16(7):1116-25. PMID:18611384[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schrader N, Koerner C, Koessmeier K, Bangert JA, Wittinghofer A, Stoll R, Vetter IR. The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking site at the nuclear pore complex. Structure. 2008 Jul;16(7):1116-25. PMID:18611384 doi:10.1016/j.str.2008.03.014
