IndraLab

Statements

Ubiquitin binds STAMBP. 6 / 8
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"To develop potent and specific inhibitors for STAMBP, we decided to employ a structure-based combinatorial Ub engineering strategy to inhibit the Ub-STAMBP protein–protein interaction ( xref ) selectively."
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"Using the STAMBP crystal structure xref (3RZU.pdb) and the structure of the nearly identical DUB domain of STAMBPL1 in complex with a di-Ub chain (2ZNV.pdb xref ), we used in silico molecular modelling to simulate the interaction between STAMBP and Ub ( xref )."
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"Because the crystal structure of AMSH bound to ubiquitin is not known, we took advantage of our structure to gain insights into possible effects the mutation may have on the structure of AMSH and its ubiquitin recognition. xref "
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"AMSH-LP has no functional SBM or MIT (microtubule interacting and transport) domain, and therefore cannot bind to other components of the ESCRT machinery, but a host of experimental studies have shown that the STAM protein connected to AMSH in a more subtle manner and serves as an activator of this enzymatic process [ xref , xref ], with the UIM domain of STAM serving as an activator in interactions with the proximal Ub of Lys63-Ub 2 and AMSH interacting with the distal Ub."
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"pdb) and the structure of the nearly identical DUB domain of STAMBPL1 in complex with a di-Ub chain, we used in silico molecular modelling to simulate the interaction between STAMBP and Ub (XREF_SUPPLEMENTARY)."
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"Biophysical characterization of ubiquitin binding to the catalytic domain of AMSH."
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