This data was extracted from Medline abstracts and full texts (when available) in an automated manner.
The table below describes different point mutations at a given position and provides links to other documents. The sentence(s) where the point mutations in NR1I3_MOUSE at position 355 were found are listed after the table.
Position 355 in 1I3 Constitutive Androstane alpha (CAR1) family
Position 415 in 1I Vitamin D3-like (VDR,PXR,CAR) family
Position 403 in 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR family
Reference #1
Ueda A, Kakizaki S, Negishi M, Sueyoshi T Mol Pharmacol 2002 Jun;61(6):1284-8.
CMX-CAR L352A and CAR E355A were constructed by replacing the BspEI / NheI fragment of CAR with synthetic oligonucleotides corresponding to amino acids 329 to 358 of CAR , encoding an alanine at either position 352 or 355 of the H12 / AF2 domain
To address this question , we mutated conserved amino acid residues in H12 / AF2 (L352A and E355A) and H3 (K187A) that contribute to the hydrophobic coregulator cleft on the surface of ligand-bound nuclear receptors (8 , 11 , 37 , 43 )
In contrast , mutations in either the H12 / AF2 domain (L352A and E355A) or H3 (K187A) completely inhibited constitutive activity , and TCPOBOP failed to restore activity to wild-type levels (Fig. 1A )
Single point mutations in H12 / AF2 (L352A or E355A) or H3 (K187A) specifically resulted in the complete loss of both constitutive and ligand-induced SRC-1 recruitment (Fig. 1B , lanes 4 to 9)
Moreover , the ability to selectively abolish constitutive activity in this mutant but not others (K205 , L352A , and E355A) (Fig. 1A and B ; Fig. 5A and B ) implies that constitutive and agonist-inducible activity have both distinct and overlapping determinants
In contrast , mutations in either the H12 / AF2 domain (L352A and E355A) or H3 (K187A) completely inhibited constitutive ac FIG
Reference #3 (Andersin T et al.): E355A
The point mutants L352A , L353A , E355A , I356A , and C357A and the AF-2 deletion reduced the basal activity by 90% or more , S358A by 75% , and G354A by only 10%
These include the reduced TCPOBOP inducibility of C357A (only 10.5-fold) and reduced loss of basal activity of E355A (only 80%) and S358A (only 60%) compared with wild-type CAR
E355A and S358A also resemble the profile of wild-type CAR , but their overall weaker interaction with TIF2 is shown by the reduced migratory distances between the supershifted complex (CAR-RXR-TIF2-DNA) and the gel shift complex (CAR-RXR-DNA)
Using standard nonsaturating TIF2 amounts (0.1 µg) , both K187A and E355A displayed a clear interaction with TIF2 in the absence of ligand
B , Heterodimers of in vitro translated CARK187A and CARE355A protein with RXR protein were formed in the presence of solvent , TCPOBOP , androstanol , or a combination of both
Reference #1 (Ueda A et al.): Glu355Ala
mCAR lost its constitutive activity after an AF2 mutation (Leu352Ala or Glu355Ala) or an AF2 deletion in a cell-based transfection assay (Choi et al. , 1997(image) )
mCAR lost its constitutive activity after an AF2 mutation (Leu352Ala or Glu355Ala) or an AF2 deletion in a cell-based transfection assay (Choi et al. , 1997)
2005, NucleaRDB.
cmbi.kun.nl), 21-Apr-2005