The TIR1 binding pocket had the highest affinity for IAA, and although 2,4-D could bind to TIR1, it was bound with weaker affinity [64].
To tune the strength of the translational inhibition, we replaced the L7Ae protein, the K-turn RNA motif, or both with variants that bound with weaker affinity.
Engineered knottin peptides 3-4A (RGD/RGD) and 3-4C (RDG/RGD) bound with weak affinity to untransfected K562 cells expressing α5β1 integrin, with IC50 values of 500±200 nM and 700±200 nM, respectively (Figure S2A and Table 1).
They bind with weaker affinity to other sites, most of which are not palindromic as any single substitution to the site generates a non-palindromic sequence.
Competitive titrations with 5 showed that the monoprotected ethidium derivatives also bind DNA, although with weaker affinity than the parent ethidium (see the ESI †).
Both bepridil and W7 bind to cNTnC·Ca2+·Sp with weaker affinity than to cNTnC·Ca2+; however, Sp binding does not preclude W7 binding (10), so one could assume that Sp, when bound, shifts the binding site for W7 to one more analogous to bepridil in the cNTnC·Ca2+·Sp·bepridil complex (4).
While the full-length PLA2 binds to membranes with a defined orientation, an engineered PLA2 fragment ΔN10 that lacks the N-terminal ten residues binds to membranes with weaker affinity and at random orientation, and exhibits ∼100-fold lower enzymatic activity compared to the full-length PLA2, indicating the key role of the N terminus in PLA2 function.
The ADP.Vi motor binds to MTs with weaker affinity than the apo/ADP motor (Imamula et al., 2007).
The absence of binding to a regular B-form DNA helix has been reported for various dsRBDs (Burd and Dreyfuss, 1994; Fierro-Monti and Mathews, 2000; Saunders and Barber, 2003), although competition binding studies revealed that some dsRBDs can also bind to dsDNA, albeit with weaker affinity (Bass et al, 1994).
Other lectins were bound with weak to moderate intensity only.
In our present study, we found that GT-4 not only binds to the GT-elements, such as GT-3 box and GT-3b but, but also bind to the MYB protein binding element MRE4 with weaker affinity.
