As this region interacts with the transmembrane part of ABC-transporters, the SDR helps to explain the selectivity and/or targeting of different NBDs to their cognate transmembrane domains.
The diferrous MauG NO structure indicated a critical role for another residue, Gln103, as this residue interacts with the proximal nitrogen of bound NO via the donation of a hydrogen bond.
AMPK might also be involved as this kinase normally interacts with p53 and tuberin to modulate cell proliferation.
Several studies focus on the role of position -6 as this residue apparently interacts with the PKA enzyme [ 3, 7].
We identified differential methylation associated with COL4A1, which is biologically important as this protein directly interacts with BMPs to modulate TGFβ regulation of myofibroblast differentiation required for wound contraction.
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6 This multifunctional protein occurs in several isoforms within cells, containing several aminoacid motifs and domains allowing it to oligomerize, as well as interact with numerous other molecules.
