3CH5

The crystal structure of the RanGDP-Nup153ZnF2 complex

Summary for 3CH5

• Entry DOI: 10.2210/pdb3ch5/pdb
• Related: 1ibr 2ebq 2ebr 2ebv 2gqe 2koc
• Descriptor: GTP-binding nuclear protein Ran, Fragment of Nuclear pore complex protein Nup153, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: ranbp2 type c2-c2 zinc finger, transport protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P62826; Nucleus, nuclear pore complex: P49791
• Total number of polymer chains: 2
• Total formula weight: 30464.19

Authors

Vetter, I.R.,Schrader, N. (deposition date: 2008-03-07, release date: 2008-07-01, Last modification date: 2024-04-03)

Primary citation

Schrader, N.,Koerner, C.,Koessmeier, K.,Bangert, J.A.,Wittinghofer, A.,Stoll, R.,Vetter, I.R.
The Crystal Structure of the Ran-Nup153ZnF2 Complex: a General Ran Docking Site at the Nuclear Pore Complex
Structure, 16:1116-1125, 2008

PubMed Abstract: 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.

PubMed: 18611384
DOI: 10.1016/j.str.2008.03.014

Experimental method

X-RAY DIFFRACTION (2.1 Å)