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 C321Q 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 C321Q in RORA_HUMAN

Point mutation:	C321Q
Cited point mutation:	C288Q
Domain:	LBD HELIX 1
General numbering (NucleaRDB):	154
Protein:	RORA_HUMAN (RORA,NR1F1, RZR)	Swiss-Prot Cross-reference table Family page
Protein isoforms	4
Other point mutations / same protein	List of mutations in RORA_HUMAN
Family alignments	1F1 ROR alpha 1F RAR-related orphan receptor (ROR,HR3) 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR
Other point mutations / same position
Reference:	Crystal structure of the human RORalpha Ligand binding domain in complex with cholesterol sulfate at 2.2 A. Kallen J, Schlaeppi JM, Bitsch F, Delhon I, Fournier B J Biol Chem 2004 Apr 2;279(14):14033-8. Epub 2004 Jan 13.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

C288Q

We hypothesized that the mutation C288Q would modify the position of Arg370 and / or of loop L1-2 (Fig. 1B ) and thus would preferentially lower the affinity of cholesterol sulfate versus cholesterol
Under these experimental conditions , the transcriptional activity of the mutant ROR alpha C288Q was found to be similar to the one elicited by ROR alpha wild type (Fig. 3A )
This unaffected transcriptional activity of the C288Q mutant probably reflects the binding of cholesterol to the mutated ROR alpha
Cos7 cells were seeded at a density of 1 x 105 cells / cm2 in 12-well plates and transiently transfected with 0.50 痢 of expression vector for ROR alpha wild type or ROR alpha mutants (C288Q and K339A , E509A) together with 1.0 痢 of ROREtkluc and as indicated under 'Materials and Methods.' 24 h after transfection , cells were collected with 250 痞 of passive lysis buffer , and luciferase activity was determined in duplicate on 20 痞 of cell extracts
B , U2OS cells were transfected as described under 'Materials and Methods' with ROR alpha wild type and ROR alpha C288Q
Results are expressed as the percentage of induction of cholesterol sulfate when compared with cholesterol for ROR alpha and ROR alpha C288Q
In contrast , the mutant C288Q did not display this improved transcriptional activity (with respect to cholesterol) when cells were treated with cholesterol sulfate (Fig. 3B )
This is consistent with the prediction that the C288Q mutant preferentially reduces the affinity of cholesterol sulfate

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