Summary information and primary citation
- PDB-id
-
3qmc;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- DNA binding protein-DNA
- Method
- X-ray (2.1 Å)
- Summary
- Structural basis of selective binding of nonmethylated
cpg islands by the cxxc domain of cfp1
- Reference
-
Xu C, Bian C, Lam R, Dong A, Min J (2011): "The
structural basis for selective binding of non-methylated
CpG islands by the CFP1 CXXC domain." Nat
Commun, 2, 227. doi: 10.1038/ncomms1237.
- Abstract
- CFP1 is a CXXC domain-containing protein and an
essential component of the SETD1 histone H3K4
methyltransferase complex. CXXC domain proteins direct
different chromatin-modifying activities to various
chromatin regions. Here, we report crystal structures of
the CFP1 CXXC domain in complex with six different CpG DNA
sequences. The crescent-shaped CFP1 CXXC domain is wedged
into the major groove of the CpG DNA, distorting the B-form
DNA, and interacts extensively with the major groove of the
DNA. The structures elucidate the molecular mechanism of
the non-methylated CpG-binding specificity of the CFP1 CXXC
domain. The CpG motif is confined by a tripeptide located
in a rigid loop, which only allows the accommodation of the
non-methylated CpG dinucleotide. Furthermore, we
demonstrate that CFP1 has a preference for a guanosine
nucleotide following the CpG motif.
