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 E355A 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 E355A in NR1I3_MOUSE

Point mutation:	E355A
Domain:	LBD HELIX 12
General numbering (NucleaRDB):	1250
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 355 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 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:	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:

E355A

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

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