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 F279A 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 F279A in VDR_HUMAN

Point mutation:	F279A
Cited point mutation:	Phe279Ala,Phe279
Domain:	LBD HELIX 5
General numbering (NucleaRDB):	560
Protein:	VDR_HUMAN (VDR,NR1I)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein	List of mutations in VDR_HUMAN
Family alignments	1I1 Vitamin D3 (VDR) 1I Vitamin D3-like (VDR,PXR,CAR) 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR
Other point mutations / same position
Reference:	The importance of the putative helices 4 and 5 of human vitamin D(3) receptor for conformation and ligand binding. Vaisanen S, Duchier C, Rouvinen J, Maenpaa PH Biochem Biophys Res Commun 1999 Oct 22;264(2):478-82.	Medline
Other point mutations / same article	List
Text source	abstract
Validation status	True positive

Relevant sentences:

Phe279

The amino acid residues Ser256 , Glu257 , Asp258 , Gln259 , Lys264 , Ser265 , Ser266 , Glu269 , Arg274 , Ser278 , and Phe279 were substituted by alanine
Our results suggest that Arg274 is important for the binding of calcitriol and probably also for the binding of the synthetic vitamin D analog MC1288 , whereas Asp258 , Gln259 , Glu269 , and Phe279 may have an important role in stabilizing the conformation of hVDR after ligand binding.

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