The phrase "allowing it to interact" is correct and usable in written English.
You can use it when describing a situation where something is permitted to engage or connect with another entity or system.
Example: "The new software update is designed with features allowing it to interact seamlessly with other applications."
Alternatives: "enabling it to engage" or "permitting it to connect".
Recently, crystal structures of a reductase variant with a four amino acid deletion in the hinge connecting the FMN and FAD domains reveal the FMN domain of reductase undergoes a structural rearrangement that separates it from the FAD domain and exposes the FMN domain, allowing it to interact with its redox partner, cytochrome P450 [28].
Watch your bird silently, talk to it, and let it out of its cage regularly, allowing it to interact with objects in the room.
When the extracellular domain binds to its ligand, the intracellular domain switches its state from inactive to active, allowing it to interact with other molecules inside of the cell, thereby initiating an intracellular signaling process.
These data suggest that cdh23 bait is correctly expressed in yeast with its Cub-LexA-VP16-tag facing the cytoplasm, allowing it to interact with prey proteins.
S1P can be secreted from the cell, allowing it to interact with G-protein-coupled receptors; alternatively, S1P or its derivatives can function intracellularly to mediate signaling activity (reviewed in 35, 36).
Our data suggest that Intβ1 is required in this context for robust activation of Ddr on the ventral TVC surface, although it is unclear if the primary role of Intβ1 is to localize Ddr to the ventral surface thereby allowing it to interact with the ventrally localized collagens.
Certainly, the modular nature of its architecture might allow it to interact with both splicing and non-splicing factors.
Additionally, human Tcf19 contains a PHD or RING finger region at its carboxyl terminus, which may allow it to interact with chromatin via methylated histone H3 (25, 42).
In a recent review Holmes and Lehman put forward the proposal that the intrinsic helical contour of tropomyosin complements the actin filament structure by having a shape that allows it to interact with all seven actins along its length [30].
It binds DNA directly through its N-terminal methyl-CpG binding domain (MBD), whereas its C-terminal transcriptional repression domain (TRD) allows it to interact with corepressors such as Sin3a, HDAC1, and HDAC2 (Nan et al., 1998).
We show that FAF1 contains a non-canonical FFAT motif that allows it to interact directly with the MSP domain of VAPB and, thereby, to mediate VAPB interaction with p97.
