Abstract
The ubiquitin-like modifier (UBL) domain of ubiquitin-like domain proteins (UDPs) interacts specifically with subunits of the 26 S proteasome. A novel UDP, ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1), has been identified as an interacting partner of the 26 S proteasome. We determined the high-resolution solution structure of the UBL domain of human UBLCP1 by nuclear magnetic resonance spectroscopy. The UBL domain of hUBLCP1 has a unique β-strand (β3) and β3-α2 loop, instead of the canonical β4 observed in other UBL domains. The molecular topology and secondary structures are different from those of known UBL domains including that of fly UBLCP1. Data from backbone dynamics shows that the β3-α2 loop is relatively rigid although it might have intrinsic dynamic profile. The positively charged residues of the β3-α2 loop are involved in interacting with the C-terminal leucine-rich repeat-like domain of Rpn1.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Humans
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Models, Molecular
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Molecular Sequence Data
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism*
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Phosphoprotein Phosphatases / chemistry*
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Phosphoprotein Phosphatases / metabolism*
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Protein Structure, Tertiary
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Solutions
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TNF Receptor-Associated Factor 2
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Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / metabolism*
Substances
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Nuclear Proteins
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PSMD2 protein, human
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Solutions
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TNF Receptor-Associated Factor 2
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Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
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Phosphoprotein Phosphatases
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UBLCP1 protein, human
Grants and funding
This work was supported by Korea Research Foundation Grant (KRF-2008-313-C00524 to W.L.), WCU (World Class University) program (R33-2009-000-10123-0) and High Field NMR Research Program of Korea Basic Science Institute. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.