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Example sentences for: af-
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The LBD utilizes a large hydrophobic cleft composed of residues along H3 and H5 to bind IDs [ 17 ] , and a smaller hydrophobic cleft that is composed of residues in the upper part of H3 and H5 and H12 (and corresponds to AF-2) to bind NR boxes [ 18 ] . Thus, agonists promote coregulator exchange by promoting the packing of H12 over the lower part of the ID binding region, an event that simultaneously completes the coactivator binding surface.
The fact that the mode of ERβ interaction with N-CoR resembles that of NRs with coactivators [ 4 ] , or with corepressors that modulate the activity of liganded NR complexes, such as RIP140 [ 10 ] , raises the possibility that ERβ may be able to recruit N-CoR and SMRT to estrogen-regulated promoters in response to agonists and that the balance of overall ERβ activity in the presence of estrogens may be regulated by competition between p160s and corepressors for the same ERβ AF-2 surface.
AF-2 Activation function 2
A number of RXR heterodimer complexes have been categorized as either permissive or non-permissive based on their responses to RXR ligands [ 1 ] . Although there are some reported discrepancies, the PPAR, FXR and NGF-IB/NURR1 complexes are generally considered permissive, while the non-permissive group includes the RAR, TR and VDR complexes (see [ 2 3 4 5 6 7 ] ). In the permissive complexes, coactivators can presumably bind to the AF-2 surface of both partners and binding to the RXR partner is stimulated by rexinoid agonists.
This sequence does not exactly conform to the LXXLL consensus, but contains features (underlined) that resemble the ERβ H12 region (L L LE ML ), and artificial ERβ interacting LXXLL peptides (293, P NLIS LLS ; D47, PL LLS LLS ), both of which bind to the ERβ AF-2 surface [ 43 44 45 46 47 ] . Moreover, the presence of a proline residue amino-terminal to the hydrophobic groups is typical of so-called class II LXXLL motifs which are found in ERβ interacting cofactors such as TRAP220 and RIP140 [ 45 ] . Finally, the unusual C-terminal hydrophobic pair (ML) has been observed in ERα and ERβ H12 [ 43 44 48 ] , and in RIP140 NR boxes [ 19 ] .
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