Words similar to lxxll
Example sentences for: lxxll
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Structure-function analysis of the NCoAs have revealed multiple copies of a signature motif, LXXLL, with conserved spacing that is required for interaction with nuclear receptors and CBP/p300 [ 99 101 ] . Intriguingly, different LXXLL motifs are required for PPARγ (Peroxisome Proliferator activated receptor γ, a gene down-regulated in Tat expressing cells; Acc# L07592, Table 1) function in response to different classes of ligands, suggesting distinct configuration of assembled complexes.
Phage display techniques have revealed that ERα and ERβ show different preferences in LXXLL binding (reviewed in [ 34 35 ] ). Moreover, some cofactors that contain LXXLL motifs show differential binding to LBDs of the ER isoforms (reviewed in [ 36 ] ). SHP binds ERα preferentially [ 37 ] , and represses ERα activity more strongly than that of ERβ.
Stat3 also contains in its N-terminus one of this motifs ( 221LAGLL 225) [ 39 ] . Moreover, Stat3 also presents a Ser at -2 position of the LXXLL sequence, which in the case of the coactivator TRBP defines selectivity for nuclear receptors [ 40 ] . Phosphorylation of Stat3 has been reported to occur only in 705Tyr and in 727Ser, allowing dimerization and full transactivating activity [ 41 ] . Whether this 219Ser next to the LXXLL motif is involved in the coactivator activity of Stat3, and the interaction of Stat3 with other coactivators only takes place in the context of Stat3 transcription factor activity or also can be part of the general mechanism of the transcription complex formation requires further studies.
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 ] .
Mutation of N-CoR to obtain a β-box sequence that more closely resembled a conventional LXXLL motif (T2402L) led to enhanced hormone-dependent interactions with ERβ and permitted novel hormone-dependent interactions with ERα (Fig.
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