1gwr: Difference between revisions
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Revision as of 11:26, 30 October 2007
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HUMAN OESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN COMPLEX WITH 17BETA-OESTRADIOL AND TIF2 NRBOX3 PEPTIDE
OverviewOverview
The activation function 2/ligand-dependent interaction between nuclear, receptors and their coregulators is mediated by a short consensus motif, the so-called nuclear receptor (NR) box. Nuclear receptors exhibit, distinct preferences for such motifs depending both on the bound ligand, and on the NR box sequence. To better understand the structural basis of, motif recognition, we characterized the interaction between estrogen, receptor alpha and the NR box regions of the p160 coactivator TIF2. We, have determined the crystal structures of complexes between the, ligand-binding domain of estrogen receptor alpha and 12-mer peptides from, the Box B2 and Box B3 regions of TIF2. Surprisingly, the Box B3 module, displays an unexpected binding mode that is distinct from the canonical, LXXLL ... [(full description)]
About this StructureAbout this Structure
1GWR is a [Protein complex] structure of sequences from [Homo sapiens] with EST as [ligand]. Structure known Active Site: ESA. Full crystallographic information is available from [OCA].
ReferenceReference
Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha., Warnmark A, Treuter E, Gustafsson JA, Hubbard RE, Brzozowski AM, Pike AC, J Biol Chem. 2002 Jun 14;277(24):21862-8. Epub 2002 Apr 5. PMID:11937504
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