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Statements

ScpA binds STAMBP. 19 / 19
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"Our results also demonstrate that Lys63-Ub 2 and the AMSH-SBM share the same binding interface within the SH3 domain of STAM2."
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"The AMSH-SBM outcompetes Lys63-Ub 2 for SH3 binding, while Lys63-Ub 2 can still bind the UIM domain of STAM2 in the presence of the AMSH-SBM."
27725184
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"Based on the NMR structure of AMSH and STAM complex (PDB ID: 5IXF) from H. sapiens , Hologne et al. considered that the interaction of AMSH-SBM and STAM-SH3 contributed to the correct positioning of polyubiquitin chains toward AMSH before cleavage [ xref , xref ]."
35883466
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"To address this question, we compared the interaction of the UIM-SH3 construct of the STAM2 protein with the SBM motif of AMSH (AMSH-SBM) or Lys63-linked diubiquitin (Lys63-Ub 2 )."
27725184
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"Here, we show that Lys63-Ub 2 can bind either the UIM or the SH3 domain without any selectivity and that the AMSH-SBM can outcompete Lys63-Ub 2 for binding with the SH3 domain."
27725184
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"Our results indicate that Lys63-Ub 2 can still bind the UIM domain when AMSH-SBM is bound to the SH3 domain of STAM2."
27725184
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"Additionally, we have solved the structure of the UIM-SH3 construct in complex with AMSH-SBM."
27725184
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"As no structural details are available yet, we tried to understand how the AMSH-SBM could interact with the SH3 domain of STAM."
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"At this point, it is worth emphasizing that the sequence length of the AMSH-SBM has a direct effect on the kinetics of binding between AMSH and SH3 (see Table 1 )."
27725184
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"Following our abovementioned results, we were seeking to understand how the AMSH-SBM could interact with the SH3 domain of STAM2 in the presence of Lys63-linked polyubiquitin chains."
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"The AMSH-P1 peptide, which contains the minimum sequence length for the AMSH-SBM, binds to SH3 with a dissociation constant of 2.0 ± 0.7 μM and a dissociation rate constant ( k off ) of 117 ± 43 s − 1[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
27725184
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"To understand the possible mechanism underlying the polyubiquitin chain cleavage by AMSH in the presence of STAM, we solved the structure of the AMSH-SBM domain in interaction with the SH3 domain of S[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As in the free state, the AMSH-SBM remains unstructured upon binding to SH3 and is located in a region delimited by the RT, n-Src loop, and the 3 10 helix."
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"The specific binding of AMSH-SBM is characterized by key residues that participate with its orientation with respect to SH3."
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"Indeed, the residues Ala228 and Lys229 of AMSH-SBM are engaged in hydrogen bonds with Asp219 of SH3, while Arg235 and Lys238 of AMSH-SBM form hydrogen bonds with Glu221 and Glu224 of SH3."
27725184
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"Our results highlight the fact that the core 235 RXXK 238 motif is critical but not essential for AMSH-SBM to bind SH3."
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"Taken together, our results demonstrate that the mutation of either one of the two lysines in the AMSH-SBM results in a negative effect in terms of binding affinity or binding kinetics."
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"Knowing that the AMSH-SBM outcompetes Lys63-linked polyubiquitin chains and that it is separated from the catalytic domain by a 16-aa-long arm, one can legitimately hypothesize a mechanism where the A[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Considering also that the affinity of AMSH for diubiquitin matches the K M value observed with the diubiquitin substrate [44] , the interaction between the AMSH-SBM and the SH3 domain of STAM2 would c[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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