Here, the Smad complex can bind to DNA directly, at so-called SBE sites (Smad binding element), but with low binding affinity, only, and can also bind to and interact with a plethora of other transcription factors, coactivators or corepressors among them transcription factors of the AP1 and Sp1 families.
In addition, another study showed that HBc can enhance host NF-kB DNA-binding ability [ 34], which suggested that HBc may bind to and interact with other host nuclear proteins to enhance or inhibit their transcriptional activator functions.
Lead is able to bind to and interact with many of the same enzymes as these metals but, due to its differing chemistry, does not properly function as a cofactor, thus interfering with the enzyme's ability to catalyze its normal reaction or reactions.
Acrosome integrity is critical when spermatozoa need to attach to the mucosa of the oviductal wall [39] and, later, when the spermatozoon reaches the ovum and has to penetrate the ovum vestments [40] and bind to and interact with the zona pellucida [35].
The I179N mutation described here does not occur at the C-terminus; however, PDZ domains do bind to, and interact with, proteins at internal, that is non C-terminal, sequences although such internal binding is rare and poorly understood [23], [32] [37].
The camelliagenin can spontaneously bind to and interact with MDH and eDNA.
Ionic interactions have been suggested as one of the primary mechanisms by which proteins bind to and interact with many GAGs.
Lead is able to bind to and interact with many of the same enzymes as these metals but, due to its differing chemistry, does not properly function as a cofactor, thus interfering with the enzyme's ability to catalyze its normal reaction(s).
We have also demonstrated that Nkd1 binds to and somehow modifies, interacts with, or stabilizes different Dvl2 isoforms.
Based on these observations, Herrero et al suggested the following sequence: trabectedin binds covalently to the DNA minor groove, the resulting adduct is recognized by the nucleotide-excision repair machinery, and then the recruited Rad13 (XPG) protein binds to DNA and interacts with the minor groove-bound drug by means of an arginine residue located in the COOH terminus.
