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We systematically identified the structure and sequence features associated with this divergence and found that most of the neomorphic positions in Gα form a ring of residues centered on the nucleotide binding site, several of which are likely to be critical for interactions with the RGS domain for its GAP function.
FtsZΔC21 lacks 21 amino acids from the C-terminus, a region believed to be critical for interactions of FtsZ with other cell division proteins [38], [39], [40], [41].
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Taken together these observations suggest that the SLBB domain in these proteins is likely to be critical for interaction with cell polysaccharides and/or sugars of the peptidoglycan.
The region of similarity shared by P. falciparum PFI1425w and other TAF7 was previously shown to be critical for interaction with the bromo domain factor Bdf1 of yeast cells [ 46].
Interestingly, this conformation positions the G183 residue that has been shown to be critical for interaction of BtpA with microtubules ([ 30] and this study), and shows that the WxxxE motif is an important structural motif in the interaction of BtpA with the microtubule network.
The crystal structure of the Ring1B-Bmi1 comprovidesvides a molecular explanation for this observation: the Arg70 residue in Ring1B that corresponds to Arg65 in Sce is thought to be critical for interaction with Bmi1 (Buchwald et al., 2006; Li et al., 2006).
The amino acids that are critical for interactions with C1q are shown in blue (D270, K322, P329, P331) (Idusogie et al., 2000).
Examination of key residues interacting between the monomers in all three models clearly showed that the amino acid residues in the N-terminus of TDP-43 are critical for interactions necessary to maintain the structure of the homodimer interface.
Two domains in the cytoplasmic tail of CD40 are critical for TRAF association and signal activation: a membrane-proximal region containing amino acids GlnGlu responsible for TRAF6 binding and a ProXGlnXThr motif that is critical for interactions with TRAF2 and TRAF3 and indirectly with TRAF5.
We found that removal of the GH3 domain prevented Reaper from interacting with MFN2, which initially suggested simply that mitochondrial localization was critical for interaction.
All NA inhibitors on the market or in clinical phases possess strong structural resemblance in those parts, which correspond to the fact that the four pockets are critical for interaction with the active site of NA.
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Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com