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1LO1

ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNA

Summary for 1LO1
Entry DOI10.2210/pdb1lo1/pdb
NMR InformationBMRB: 5363
Descriptor5'-D(*GP*CP*TP*CP*AP*AP*GP*GP*TP*CP*AP*CP*G)-3', 5'-D(*CP*GP*TP*GP*AP*CP*CP*TP*TP*GP*AP*GP*C)-3', Steroid hormone receptor ERR2, ... (4 entities in total)
Functional Keywordsestrogen related receptor 2, dna binding domain, herr2, hormone nuclear receptor, hormone-growth factor receptor-dna complex, hormone/growth factor receptor/dna
Biological sourceHomo sapiens (human)
Cellular locationNucleus (Potential): O95718
Total number of polymer chains3
Total formula weight19223.11
Authors
Gearhart, M.D.,Holmbeck, S.M.A.,Evans, R.M.,Dyson, H.J.,Wright, P.E. (deposition date: 2002-05-05, release date: 2003-04-22, Last modification date: 2024-05-22)
Primary citationGearhart, M.D.,Holmbeck, S.M.A.,Evans, R.M.,Dyson, H.J.,Wright, P.E.
Monomeric Complex of Human Orphan Estrogen Related Receptor-2 with DNA: A Pseudo-dimer Interface Mediates Extended Half-site Recognition
J.Mol.Biol., 327:819-832, 2003
Cited by
PubMed Abstract: While most nuclear receptors bind DNA as homo or heterodimers, the human estrogen related receptors (hERRs) are members of a subfamily of orphan receptors that bind DNA as monomers. We have determined the solution structure of the DNA binding domain (DBD) of hERR2 bound to its cognate DNA. The structure and base interactions of the core DBD are similar to those of other nuclear receptors. However, high-affinity, sequence-specific DNA binding as a monomer necessitates formation of additional base contacts outside the core DBD. This is accomplished using a modified guanosine-binding "AT-hook" within the C-terminal extension (CTE) flanking the DBD, which makes base-specific minor groove interactions. The structure of the CTE is stabilized both by interactions with the DNA and by packing against a region of the core DBD normally reserved for dimerization. This pseudo-dimer interface provides a basis for the expansion of DNA recognition and suggests a mechanism through which dimerization may have evolved from an ancestral monomeric receptor.
PubMed: 12654265
DOI: 10.1016/S0022-2836(03)00183-9
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227111

數據於2024-11-06公開中

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