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Nucleotide binding and oligomerization

Nucleotide-binding and oligomerization domain (NOD)-like receptor (NLR) proteins... [Pg.186]

The oligomeric structure of the heterotrimeric G proteins increases the complexity and diversity of their signaling mechanisms. The intrinsic GTP cycle is direcdy associated with a cycle of subunit dissociation in which the oc subunit (which contains the nucleotide-binding site) can dissociate from a stable fiy dimer (Fig. 1). In the inactive GDP-bound state, high affinity between the oc and /fy subunits favors association. When GTP is bound, the affinity between subunits is lowered and dissociation is promoted. This allows both oc and fty subunits to act as coordinate or diverse regulators of downstream targets. Reassociation of the subunits inhibits downstream... [Pg.191]

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Nucleotides and

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