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The PH domain of Son of sevenless (SOS) and PX domains of p47phox have previously been shown to possess a phosphoinositide-binding pocket and a second anion binding pocket which enables them to interact with PA facilitating plasma membrane recruitment [40], [41].
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Im et al. [64] showed that Osh4p as other lipid transfer proteins contains a lipid-binding pocket which enables uptake of sterols from a membrane and release at another one.
These observations demonstrate a degree of plasticity within the pocket, which enables it to accommodate different residues.
One approach is to identify molecules that occupy the pterin binding pocket which is distinct from the pABA binding pocket that binds sulfonamides.
FhGAPDH lacks a binding pocket which has been exploited in the design of novel antitrypanosomal compounds.
The kinase domain has a broad substrate binding pocket, which preferentially recognizes double-stranded substrates with recessed 5′ termini.
Majority of small molecule kinase inhibitors reversibly occupy the ATP binding pocket, which means that they are ATP-competitive inhibitors.
In comparison with the S5 S1 pockets, the prime-side binding pockets, which interact with the P′ residues downstream of the cleavage junction, are less well defined.
Such conformational changes facilitate the formation of an ephrin-binding pocket which accommodates a phenylalanine residue, Phe120ephrinB2.
Additionally, the SRL is proposed to host several cation-binding pockets, which could facilitate platinum coordination.
The anchor residues for HLA-A2 fit into narrow and specific-binding pockets, which allow almost only P2 Met and Leu for pocket B and Pc Val and Leu for pocket F (Guo et al., 1993).
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