The first two domains, which have been implicated in active-site pocket formation and acetyl-CoA binding, are connected to the third domain through the α-helical interdomain.
In the MF category, 56.25% of GO annotations were connected to transcription factor binding or transcription regulator activity, while 3 out of 16 of the GO annotations were related to DNA binding.
The crystals were connected to the substrate surface by ordered nanolayers, indicating the existence of a continuous binding between the two materials.
In fact, in Hsp90-type chaperones, the ATP binding domain is connected to the middle domain via a divergent linker region.
The authors find that a hexa-peptide of the PKA kinase, a known regulator of RyR2, has a very high affinity for RyR2, in the nano-molecular range, and that its binding site is connected to two known disease-associated residues (A77 and R176) through a "path" of residues predicted to be "energy responsive" through ENM calculations.
The three-dimensional structure of Rsd in complex with σ70 region 4 reveals that the sigma-binding surface is connected to exposed cavities, which might act as binding pockets for small regulatory molecules.
In particular, in the access and binding phases D407 is connected to R971 via a cluster of four water molecules, while in the extrusion phase this proton path is blocked by the two side chains of V411 and L944 which are conserved as hydrophobic residues in the AcrB-like family (Fig. S1).
It consists of an extracellular ligand binding region, which is connected to the cytosolic region through a hydrophobic transmembrane domain.
This protein consists of a flavodoxin-like FMN-binding domain that is connected to a cytochrome p450 reductase-like domain, including a FAD binding pocket and an NADP(H) binding site (Fig. S5).
We directly show that lipid binding of this mutant is connected to an open lid conformation demonstrating the impact of the exposed amino acid residues and their participation in binding at the water-lipid interface.
