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This interaction involves highly conserved hydrophobic and polar residues that tightly interact with the BC groove.
Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 Å putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
Both fluoroquinolones were comparable in their ability to photo-induce DNA strand breaks or oxidative damage to purines and pyrimidines in supercoiled plasmid DNA, but agarose gel electrophoresis showed that BAYy3118 photoproducts could tightly interact with supercoiled plasmid DNA while lomefloxacin ones only induced strand breaks.
The plant growth-hormone pathways tightly interact with light signalling and the diurnal cycle in the control of plant growth.
Furthermore, N. meningitidis has a propensity to tightly interact with endothelial cells and to cross the blood-brain barrier, resulting in fulminant meningococcal meningitis [4].
Detailed in vitro characterization confirmed that these binders tightly interact with EGFP.
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We identify a class of Reb1 sites where the proximal −1 nucleosome tightly interacts with Reb1 and maintains unidirectional transcription.
Having a rather low affinity to OCPO (Kd ~35 µM), FRP tightly interacts with OCPR and its analogs with separated domains (Kd ~1 3 µM)24,32.
Sluchanko, N. N. et al. The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP.
The helical domain, containing five helices, tightly interacts with the catalytic domain, and is likely critical for catalytic activity due to its association with organizing the active site.
HerA forms an ASCE hexamer that tightly interacts with a NurA dimer, with each NurA protomer binding three adjacent HerA HAS domains.
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