The <scp>MECP2‐TRD</scp> domain interacts with the <scp>DNMT3A‐ADD</scp> domain at the <scp>H3</scp> ‐tail binding site-Reference-Cited by-同舟云学术

The MECP2‐TRD domain interacts with the DNMT3A‐ADD domain at the H3 ‐tail binding site

Published:2022-12-29 Issue:1 Volume:32 Page:
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Kunert Stefan¹,Linhard Verena²,Weirich Sara¹,Choudalakis Michel¹,Osswald Florian¹,Krämer Lisa¹,Köhler Anja R.¹,Bröhm Alexander¹,Wollenhaupt Jan³,Schwalbe Harald²,Jeltsch Albert¹^ORCID

Affiliation:

1. Institute of Biochemistry and Technical Biochemistry University of Stuttgart Stuttgart Germany

2. Center for Biomolecular Magnetic Resonance (BMRZ), Institute for Organic Chemistry and Chemical Biology Goethe University Frankfurt Germany

3. Macromolecular Crystallography Group Helmholtz‐Zentrum Berlin Berlin Germany

Funder

Deutsche Forschungsgemeinschaft

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4542

Reference63 articles.

1. Towards automated crystallographic structure refinement with phenix.refine

2. Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2

3. MeCP2: the long trip from a chromatin protein to neurological disorders

4. Dnmt3a and Dnmt3b Are Transcriptional Repressors That Exhibit Unique Localization Properties to Heterochromatin

5. Genomic profiling of DNA methyltransferases reveals a role for DNMT3B in genic methylation

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1. ADD domains—A regulatory hub in chromatin biology and disease;Chromatin Readers in Health and Disease;2024

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3. Growth retardation associated with a novel DNMT3A variation in a Chinese boy: A Case Report;2023-07-28

4. Unveiling the methyl transfer mechanisms in the epigenetic machinery DNMT3A-3 L: A comprehensive study integrating assembly dynamics with catalytic reactions;Computational and Structural Biotechnology Journal;2023