PMID- 10581239
OWN - NLM
STAT- MEDLINE
DCOM- 20000131
LR  - 20081120
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 23
DP  - 1999 Dec 1
TI  - Solution structure of the methyl-CpG-binding domain of the methylation-dependent 
      transcriptional repressor MBD1.
PG  - 6653-61
AB  - CpG methylation in vertebrates is important for gene silencing, alterations in
      chromatin structure and genomic stability, and differences in the DNA-methylation
      status are correlated with imprinting phenomena, carcinogenesis and embryonic
      development. Methylation signals are interpreted by protein factors that contain 
      shared methyl-CpG-binding domains (MBDs). We have determined the solution
      structure of the MBD of the human methylation-dependent transcriptional repressor
      MBD1 by multi-dimensional heteronuclear NMR spectroscopy. It folds into an
      alpha/beta-sandwich structure with characteristic loops. Basic residues conserved
      in the MBD family are largely confined to one face of this fold and a flexible
      loop, which together form a large positively charged surface. Site-directed
      mutagenesis and chemical shift changes upon complexing with a methylated DNA
      facilitated identification of this surface as the DNA interaction site. In
      addition to three basic residues, conserved Tyr34 and Asp32 were shown to be
      important for the DNA binding.
FAU - Ohki, I
AU  - Ohki I
AD  - Graduate School of Biological Sciences, Nara Institute of Science and Technology,
      8916-5 Takayama, Ikoma, Nara 630-0101, USA.
FAU - Shimotake, N
AU  - Shimotake N
FAU - Fujita, N
AU  - Fujita N
FAU - Nakao, M
AU  - Nakao M
FAU - Shirakawa, M
AU  - Shirakawa M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Chromosomal Proteins, Non-Histone)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (MBD1 protein, human)
RN  - 0 (MECP2 protein, human)
RN  - 0 (Methyl-CpG-Binding Protein 2)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (Transcription Factors)
RN  - EC 2.5.1.18 (Glutathione Transferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - *Chromosomal Proteins, Non-Histone
MH  - DNA Methylation
MH  - DNA-Binding Proteins/*chemistry
MH  - Escherichia coli/metabolism
MH  - Glutathione Transferase/metabolism
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Methyl-CpG-Binding Protein 2
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Protein Binding
MH  - Recombinant Fusion Proteins
MH  - Repressor Proteins/*chemistry
MH  - Sequence Homology, Amino Acid
MH  - Transcription Factors
PMC - PMC1171728
EDAT- 1999/12/03 00:00
MHDA- 1999/12/03 00:01
CRDT- 1999/12/03 00:00
PHST- 1999/12/03 00:00 [pubmed]
PHST- 1999/12/03 00:01 [medline]
PHST- 1999/12/03 00:00 [entrez]
AID - 10.1093/emboj/18.23.6653 [doi]
PST - ppublish
SO  - EMBO J. 1999 Dec 1;18(23):6653-61. doi: 10.1093/emboj/18.23.6653.