Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 278, Issue 22, Pages 20225-20234Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M300459200
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Funding
- NCRR NIH HHS [RR13030] Funding Source: Medline
- NIDDK NIH HHS [R01 DK068139] Funding Source: Medline
- NIGMS NIH HHS [R01 GM055508, R01 GM55508, R01 GM060919, 1R01 GM60919] Funding Source: Medline
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Ubiquitylated proteins are directed into a large number of different cellular pathways through interactions with effector proteins that contain conserved ubiquitin binding motifs. Here, we report the solution structure and ubiquitin binding properties of one such motif, the Npl4 zinc finger or RanBP2/Nup358 zinc finger (NZF) domain. Npl4 NZF forms a compact module composed of four antiparallel beta-strands linked by three ordered loops. A single zinc ion is coordinated by four conserved cysteines from the first and third loops, which form two rubredoxin knuckles. Npl4 NZF binds specifically, but weakly, to free ubiquitin using a conserved (TF14)-T-13 dipeptide to interact with the Ile-44 surface of ubiquitin. Our studies reveal the structure of this versatile class of protein binding domains and provide a means for identifying the subset of NZF domains likely to bind ubiquitin.
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