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 T302A 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 T302A in NR1H3_HUMAN

Point mutation:	T302A
Domain:	LBD HELIX 5
General numbering (NucleaRDB):	556
Protein:	NR1H3_HUMAN (NR1H3,LXR)	Swiss-Prot Cross-reference table Family page
Protein isoforms	2
Other point mutations / same protein	List of mutations in NR1H3_HUMAN
Family alignments	1H3 Oxysterol LXR alpha 1H Ecdysone-like (ECR,LXR,FXR) 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR
Other point mutations / same position	Position 263 in 1 Thyroid hormone like (TR,RAR,ROR,PPAR,VDR family
Reference:	Molecular determinants of LXRalpha agonism. Wang M, Thomas J, Burris TP, Schkeryantz J, Michael LF J Mol Graph Model 2003 Nov;22(2):173-81.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

T302A

The sense strand oligonucleotide sequences are as follows: F254A GGCCCGTCAGCAGCGCGCTGCCCACTTCACTGAGC F257A GCAGCGCTTTGCCCACGCCACTGAGCTGGCCATC M298A GACCTCTGCGATCGAGGTGGCGCTTCTGGAGACATCTCG L299A GCGATCGAGGTGATGGCTCTGGAGACATCTCGGAGG E301A CGAGGTGATGCTTCTGGCGACATCTCGGAGGTACAACC T302A GCTTCTGGAGGCATCTCGGAGGTACAACC R305L GCTTCTGGAGACATCTCGGCTGTACAACCCTGGG F315A CACTTCCTCAAGGATGCCAGTTATAACCGGGAAG L316A GGAGTGAGAGTATCACCTTCGCCAAGGATTTCAGTTATAACCGGG L331A GGAAGACTTTGCCAAAGCAGGGGCGCAAGTGGAATTCATCAA F335A GCAGGGCTGCAAGTGGAAGCCATCAACCCCATCTTCG H421A GGACCCTGAGCAGCGTCGCCTCAGAGCAAGTGTTTGC Q424A GCAGCGTCCACTCAGAGGCAGTGTTTGCACTGCGTCTGC L439A GCTCCCACCGCTGGCCTCTGAGATCTGGGATGTGC I442A GCTGCACATCCCAGGCCTCAGAGAGCAGCGGTGGG W443Y CACCGCTGCTCTCTGAGATCTACGATGTGCACGAATG Mutagenesis was confirmed by sequence analysis
A T302A substitution resulted in a universal increase in efficacy of the Gal4-LXR alpha response to all three ligands where the most significant increase occurred in response to 22RHC
Based on evidence of C---H毽慈 hydrogen bonds in nuclear receptors [22 ] , we suggest that T302 forms a weak hydrogen bond with I313 and that T302A acts as a constitutively active mutant by this mechanism

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