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Influence of PEG-modified lipids on lectin binding and the formation of protocellular junctions.
Protein binding and the formation of transporters are decisive factors in the distribution and excretion of PFCs [15, 115].
For DAT, previous molecular dynamics (MD) simulations have identified structural elements important for substrate binding and the formation of an occluded state [37], [38].
The function of the NAC domain has been associated with nuclear localization, DNA binding and the formation of homo or heterodimers with other NAC domain-containing proteins [ 19].
NAC domain has been implicated in nuclear localization, DNA binding, and the formation of homodimers or heterodimers with other NAC domain proteins [ 11- 16].
The high-level expression of a core-glycosylated ABCB6 with a correct molecular mass, the specific Mg2+-dependent ATP binding and the formation of a catalytic intermediate strongly argue against this possibility.
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Such studies have shown that two adjacent regions of AG, the MADS domain and I region, are sufficient for DNA binding and for the formation of either homodimers [ 31] or heterodimers with the MADS domain protein SEPALLATA1 (SEP1) [ 32].
The evolutionary diversification of such a binding surface(s) then resulted in a gain of new binding partners and the formation of novel MAGE complexes with RING-finger proteins (Figure 9B) ([14]; our unpublished data).
cPKC phosphorylation of S39 inhibits actin binding and drives the formation of a complex between phosphorylated fascin-1 and active cPKC, resulting in a diffuse cytoplasmic distribution of fascin-1 [ 18, 20].
Firstly, phosphorylation alters the disposition of the central membrane-anchoring α-helix with respect to the membrane which could modify how the proline-rich region is presented to the cytoplasm for binding; and secondly, the formation of salt-bridges involving the phosphorylated threonines and basic residues within the proline-rich region could reduce its flexibility [ 23].
Only for as high concentrations as 10 mol% lipopolymer, lectin binding and accordingly the formation of protocellular junctions is indeed influenced by the ligand shielding effect for the majority of vesicles.
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