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Sequence alignments and 3D molecular modelling of human type II cystatins indicate that this motif forms a 'back-side loop' located opposite the papain-binding surface.
The Arg residue of this motif forms a salt bridge (ionic lock) with Glu6.30 of TM6 that stabilizes the GPCR inactive state [28].
Here we show that Hfq belongs to the large family of Sm and Sm-like proteins: it contains a conserved sequence motif, known as the Sm1 motif, forms a doughnut-shaped structure, and has RNA binding specificity very similar to the Sm proteins.
The independently expressed central TSR of murine ADAMTS-1 required 0.46 to 0.66 M NaCl for elution from a heparin affinity column, indicating that this motif forms a functional heparin-binding unit [ 16].
The cysteine residue of this motif forms a conserved intramolecular disulfide bridge with a second conserved cysteine residue located in sialylmotif L. This S-S bond is essential for correct folding and enzymatic activity of ST8Sia [ 28].
Analysis of the Cep3 structure shows that this motif forms a disordered loop between residues 570 and 587, the base of which is directly adjacent to the N-terminal of the protein, where the linker and zinc cluster emerge (Fig 5A).
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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.
The ACGT core motif forms an important class of cis-elements implicated in a variety of functions.
In addition, the conserved Trp117 residue of the hash motif forms an important π-stacking interaction with the hydantoin moiety.
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].
The YSNS motif formed a β turn crucial for biological activity.
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