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Exact(5)
Similar to observations in the crystal structure of opsin the arginine of the DRY motif in TMH3 (in the TSHR an ERW motif) forms an H-bond interaction with the Gαq backbone at Y350 in the α5 C-terminal tail.
In addition, the conserved Trp117 residue of the hash motif forms an important π-stacking interaction with the hydantoin moiety.
The ACGT core motif forms an important class of cis-elements implicated in a variety of functions.
Closer inspection of the TRPM7 dimeric kinase domain structure revealed that the dimerization motif forms an extended α-helix which undergoes extensive interactions with a region in the kinase domain of the other monomer termed the 'dimerization pocket' [ 22].
During vesicular fusion, STX is considered to be in the "open" conformation in which its SNARE motif forms an extended and intertwined four α-helix bundle structure with other members of the SNARE complex (SNAP-25 and synaptobrevin 2).
Similar(55)
The Arg residue of this motif forms a salt bridge (ionic lock) with Glu6.30 of TM6 that stabilizes the GPCR inactive state [28].
As shown in Figure 1, the crystal structure of 2F5 Fab in complex with its epitope peptide reveals that the 664DKW666 core motif forms a β turn conformation (Bryson et al., 2001).
Furthermore, the Asp of the DRY motif forms a hydrogen bond with a Ser and not the corresponding Tyr of ICL2.
An, (GA n, and (GS n conform to beta-sheet structures that impart tensile strength, whereas repeating GPGXn motifs form beta-turns that confer extensibility, and the (GGX n motif forms a 310 helix [ 4].
Thioredoxin reductase (TrxR) has also been identified as a target, although in the case of TrxR the quinol motif forms a bond with a nucleophilic selenocysteine residue in the active site.
The validity of the predicted eh1 structure is strongly supported by a recent crystallographic study showing that the Goosecoid eh1 motif forms a short amphipathic α-helix when bound to the WD domain of TLE1 [ 29].
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