IndraLab

Statements

USP15 binds DUSP. 11 / 11
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sparser
"One of five UbVs selected for binding to USP11-DUSP exhibited slight cross-reactivity to USP15-DUSP (11D."
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"The DUSP domain of USP15 is formed from approximately 120 amino acid residues, with a defined α1-β1-α2-β2-α3-β3 secondary structure."
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"We were successful in producing the USP4-DUSP, USP11-DUSP, USP15-DUSP, USP20-DUSP2 and USP33-DUSP2 recombinant proteins in Escherichia coli and purified them to near homogeneity from the soluble fract[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"DNA sequences encoding the following residues from each USP were cloned into a pET-21b vector using Gibson Assembly 45 : USP4-DUSP, 8–129; USP15-DUSP, 1–125; USP11-DUSP, 71–191; USP20-DUSP1, 687–780; [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"WT*), with two USP15-DUSPs (DUSP and DUSP*) bound at asymmetrical positions along this dimer ( Figure 2 (A))."
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"As expected, sequence analysis revealed that UbVs selected for binding to USP15-DUSP closely resembled the parental UbV."
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"For USP15-DUSP, seven UbVs appeared to be absolutely specific (15D."
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"For USP15-DUSP and USP33-DUSP2, the best UbVs exhibited affinities in the low nanomolar range (K D ∼ 10 nM), whereas for USP11-DUSP and USP20-DUSP2, affinities were in the mid-nanomolar range (K D ∼ 1[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"1 to explore whether binding to the USP15-DUSP could serve as an alternative means to inhibit catalytic activity."
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"Although the affinity of USP15-DUSP UbVs were high for the USP15-DUSP, UbVs for the four other DUSPs showed lower affinities for their cognate DUSPs suggesting that N-terminal substitutions in UbVs ma[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The DUSP amino acid sequence alignment was conducted with Clustal Omega web server 43 and aligned to the structure of USP15-DUSP (PBD:3T9L) with ESPript 3.0 44 to better define all structural elements[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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