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 K187A 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 K187A in NR1I3_MOUSE

Point mutation:	K187A
Domain:	LBD HELIX 3
General numbering (NucleaRDB):	351
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 187 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 187 in 1I3 Constitutive Androstane alpha (CAR1) family Position 241 in 1I Vitamin D3-like (VDR,PXR,CAR) family Position 234 in 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR family
Reference:	A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activity. Dussault I, Lin M, Hollister K, Fan M, Termini J, Sherman MA, Forman BM Mol Cell Biol 2002 Aug;22(15):5270-80.	Medline
Other point mutations / same article	List
Text source	HTML and PDF full texts
Validation status	True positive

Relevant sentences:

K187A

The primers used were as follows (only the oligonucleotides representing the upper DNA strand are shown): mouse CAR K187A , 5'-ATCATCAAGTTCACCGCGGATCTGCCGCTCTTC-3' ; CAR K205E , 5'-ACCAGATCTCCCTTCTCGAGGGAGCGGCTGTGGAA-3' ; CAR loop , an insertion of three alanine residues between E345 and L346 , 5'-CTTCAGCGCTTGGAGGAAGCGGCCGCACTGTCTGCTATGACGCCG-3' ; CAR C-terminal extension , an insertion of four alanines at the end of CAR , 5'-CTCGGGGAGATTTTGCAGTGCGGCCGCGGCATGAGGCCCAGGCTTGCAT-3' ; RXR K285A , 5'-CTGGTGGAGTGGGCCGCGCGAATCCCACACTTCTCA-3' ; SRC-1 RID1m (amino acids 633 to 637 [LVQLL] , GenBank accession no
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)
Mutation of either K187A in CAR or K285A in RXR strongly reduced the association with SMRT (Fig. 3D , lanes 3 and 4) , and the combination of both mutations completely abolished the interaction (Fig. 3D , lane 5)
The primers used were as follows (only the oligonucleotides representing the upper DNA strand are shown): mouse CAR K187A , 5 -ATCATCAAGTT CACCGCGGATCTGCCGCTCTTC-3 ; CAR K205E , 5 -ACCAGATCTCCCT TCTCGAGGGAGCGGCTGTGGAA-3 ; CAR loop , an insertion of three alanine residues between E345 and L346 , 5 -CTTCAGCGCTTGGAGGAAGCG GCCGCACTGTCTGCTATGACGCCG-3 ; CAR C-terminal extension , an insertion of four alanines at the end of CAR , 5 -CTCGGGGAGATTTTGCAG TGCGGCCGCGGCATGAGGCCCAGGCTTGCAT-3 ; RXR K285A , 5 -CTG GTGGAGTGGGCCGCGCGAATCCCACACTTCTCA-3 ; SRC-1 RID1m (amino acids 633 to 637 [LVQLL] , GenBank accession no
In contrast , mutations in either the H12 / AF2 domain (L352A and E355A) or H3 (K187A) completely inhibited constitutive ac
FIG

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