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2LHN

RNA-binding zinc finger protein

Summary for 2LHN
Entry DOI10.2210/pdb2lhn/pdb
NMR InformationBMRB: 17858
DescriptorNuclear polyadenylated RNA-binding protein NAB2, ZINC ION (2 entities in total)
Functional Keywordsrna-binding protein, nuclear protein
Biological sourceSaccharomyces cerevisiae S288c (Baker's yeast)
Cellular locationNucleus: P32505
Total number of polymer chains1
Total formula weight9424.02
Authors
Brockmann, C.,Neuhaus, D.,Stewart, M. (deposition date: 2011-08-12, release date: 2012-06-27, Last modification date: 2024-05-01)
Primary citationBrockmann, C.,Soucek, S.,Kuhlmann, S.I.,Mills-Lujan, K.,Kelly, S.M.,Yang, J.C.,Iglesias, N.,Stutz, F.,Corbett, A.H.,Neuhaus, D.,Stewart, M.
Structural Basis for Polyadenosine-RNA Binding by Nab2 Zn Fingers and Its Function in mRNA Nuclear Export.
Structure, 20:1007-1018, 2012
Cited by
PubMed Abstract: Polyadenylation regulation and efficient nuclear export of mature mRNPs both require the polyadenosine-RNA-binding protein, Nab2, which contains seven CCCH Zn fingers. We describe here the solution structure of fingers 5-7, which are necessary and sufficient for high-affinity polyadenosine-RNA binding, and identify key residues involved. These Zn fingers form a single structural unit. Structural coherence is lost in the RNA-binding compromised Nab2-C437S mutant, which also suppresses the rat8-2 allele of RNA helicase Dbp5. Structure-guided Nab2 variants indicate that dbp5(rat8-2) suppression is more closely linked to hyperadenylation and suppression of mutant alleles of the nuclear RNA export adaptor, Yra1, than to affinity for polyadenosine-RNA. These results indicate that, in addition to modulating polyA tail length, Nab2 has an unanticipated function associated with generating export-competent mRNPs, and that changes within fingers 5-7 lead to suboptimal assembly of mRNP export complexes that are more easily disassembled by Dbp5 upon reaching the cytoplasm.
PubMed: 22560733
DOI: 10.1016/j.str.2012.03.011
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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