CcmF has a WWD motif (see Figure 1) that is proposed to interact with heme, via hydrophobic interactions, on the periplasmic side of the membrane (this heme molecule is transferred from CcmE to the cytochrome).
During DNA translocation, the nuclease domain was proposed to interact with DNA through electrostatic interactions at a second DNA-binding site located at a surface opposite to the nuclease active site.
These positively selected residues have only one residue that overlaps with those proposed to interact with NKG2D, thus suggesting the interaction with molecules other than NKG2D.
Due to structural mimicry SifA has further been proposed to interact with G-proteins.
The cytosolic domain of Sec61β has been proposed to interact with ribosomes or exocyst complexes (Levy et al., 2001; Lipschutz et al., 2003; Toikkanen et al., 2003).
Neurofilaments (NFs) have been proposed to interact with one another through mutual steric exclusion of their unstructured C-terminal "sidearm" domains, producing order in axonal NF distributions and conferring mechanical strength to the axon.
and AcCYS (43 135 a.a).. Three conservative regions, proposed to interact with cysteine protease, were found in SiCYS-N, Orzyacystatin I, CeCPI, and AcCYS: a G residue near the N-terminus, a central QXVXG motif in the first hairpin loop, and a W residue in the second hairpin loop near the C-terminus putatively forming a tripartite wedge.
Another protein that has been proposed to interact with PilQ is PilC.
Since T-548 lacks the domain proposed to interact with α7-nAChR, this truncated AChE molecule predictably does not exhibit an ability to bind to the receptor.
Conversely, NCp9 binding to the G4-DNA substrate easily shifts to an aggregated state, unlike NCp7 [29], and it is proposed to interact with RNA more stably than NCp7 [17].
