Based on our structures, we engineered a mutant that deacetylates peptides by using nicotinic acid adenine dinucleotide (NAAD) as a cosubstrate and is inhibited by nicotinic acid.
We also find that an ILY-derived peptide based on our structure disrupts the interface and competes for pore formation.
Based on our structures, we additionally designed a R81A/Y87F double mutant that we expected to have the strongest effect.
Based on our structure, we describe a two-fold autoinhibition of Parkin, where the linker helix blocks E2 access to RING1, and the UPD blocks access to Cys431 in RING2.
Based on our structure modeling, the common mechanistic denominator for the R179H and R258H mutations described in ARCD [ 10] is most likely the destabilization of the F-actin inter-strand interface.
To test the contribution of the CT domain to MCAK activity and function, we designed a system to generate an inducible covalent CT domain-motor complex in vitro based on our structure to control for the displacement of the CT domain from the motor domain.
Based on our structure, the existence of a kink in the middle of the peptide, which breaks it into two helices allows the peptide to undergo structural changes from α-helix to β-sheet once the two halves come close to one another.
We have discussed several possible mechanisms of autoinhibition of mDia1 based on our initial structure and proposed that structural hindrance between actin filament and the bridge elements, which occurs in the geometry of the autoinhibitory state, is the likely one.
Based on our 3D structure analysis, residue 267 is in a protein structural core; hence, this experiment directly showed that RNA editing in a structural core governs the stability of a protein.
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