NucleaRDB: Extraction of mutation data from the literature

2005, NucleaRDB.

This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation L352A was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation L352A in NR1I3_MOUSE

Point mutation:	L352A
Domain:	LBD HELIX 12
General numbering (NucleaRDB):	1247
Protein:	NR1I3_MOUSE (Nr1i3,Ca)	Swiss-Prot Cross-reference table Family page
Protein isoforms	2
Other point mutations / same protein / same position	Point mutations at position 352 in NR1I3_MOUSE
Other point mutations / same protein	List of mutations in NR1I3_MOUSE
Family alignments	1I3 Constitutive Androstane alpha (CAR1) 1I Vitamin D3-like (VDR,PXR,CAR) 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR
Other point mutations / same position	Position 352 in 1I3 Constitutive Androstane alpha (CAR1) family Position 412 in 1I Vitamin D3-like (VDR,PXR,CAR) family Position 400 in 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR family
Reference:	The critical role of carboxy-terminal amino acids in ligand-dependent and -independent transactivation of the constitutive androstane receptor. Andersin T, Vaisanen S, Carlberg C Mol Endocrinol 2003 Feb;17(2):234-46.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	True positive

Relevant sentences:

L352A

The panel of ligand inducibility on the DR4-type RE (Fig. 3A(image) , top) indicated that only L352A and the AF-2 deletion lost their responsiveness to TCPOBOP
The inverse agonistic effect of androstanol was completely lost with L352A , L353A , I356A , C357A , and the AF-2 deletion
Interestingly , with L352A , L353A , I356A , and the AF-2 deletion androstanol became slightly agonistic
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%
A minor difference was found also concerning a responsiveness of L352A to TCPOBOP , which was found to be statistically significant on the PBREM but not to the DR4-type RE
Finally , L352A , L353A , I356A , and the AF-2 deletion showed no interaction with TIF2 irrespective of ligand presence
This indicates that the supershift assay may not be sensitive enough to detect the ligand modulation of the low basal activity of the mutants L352A , L353A , and I356A
This reduction was not as drastic as observed with the mutants L352A , L353A , I356A , and C357A and the AF-2 deletion (Fig. 3(image) )
For the second hypothesis C357 was mutated into serine and tyrosine , Y336 was mutated into alanine , cysteine , and phenylalanine , and the point- mutants Y336A / C357A , Y336C / C357Y , and L352A / C357A were created
All three double-point mutants , Y336A / C357A , Y336C / C357Y , and L352A / C357A , showed nearly abolished response to ligand , which was expected because of the profile of the individual mutants Y336C , C357Y , and L352
Interestingly , C357A / Y336A and L352A / C357A reduced the basal activity of CAR by 80-90% , whereas Y336C / C357Y did not influence it significantly

F.Horn (nucleardbcmbi.kun.nl), 21-Apr-2005