ZnuA, a periplasmic zinc-binding protein that allows the influx of Zn2+, has been described as a membrane and macromolecules stabilizer [ 63, 64], and also as antioxidant [ 65].
At the structural level, one can also wonder about the actin binding proteins that allow F-actin stabilization in aligned filopodia?
The first option uses a miniaturized form of the extracellular matrix molecule agrin (mini-agrin), which is not homologous to LM-211, but shares binding properties with the protein that allow it to restore the mechanical linkage between muscle fibre and basement membrane.
As the CCND1 promotor does not contain an estrogen response element, ER needs to interact with NFκB proteins that allow the binding of the complex to NFκB response elements in the promotor of CCND1.
SSB is a heterotetrameric, single-stranded DNA binding protein that melts secondary structure in ssDNA, thereby allowing RecA monomers to form an active nucleoprotein filament [24].
We describe targeting signals in the N-terminal of DAAM1 (distinct from the Dvl2 binding domain) that allows for targeted protein function.
To further investigate the role of oncogenic RAS signaling in the differential induction of cell death in response to DNA damage or proteasome inhibition, we used a 4-hydroxytamoxifen (4OHT -inducible oncogenic RAS fusion protein with estrogen receptor hormone binding domain that allows rapid and titratable induction of downstream signals emanating directly from the mutant RAS protein.
The experiments revealed a vesicle protein called Upa1 that contains a new type of binding site that allows Upa1 to bring an important RNA-binding protein to the surface of vesicles.
The basic region, which consists of approximately 17 amino acids and is located at the N-terminus of the domain, is a DNA-binding region that allows HLH proteins to bind to a consensus hexanucleotide E-box (CANNTG) [ 5, 6].
These amphiphilic isomers share the same chemical nature, providing versatile nonspecific binding reactivity that allows to probe hidden regulatory residues on a given protein surface.
