1m18: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_1m18| PDB=1m18 | SCENE= }} | {{STRUCTURE_1m18| PDB=1m18 | SCENE= }} | ||
===LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA=== | ===LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA=== | ||
{{ABSTRACT_PUBMED_12559907}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/H2A1_XENLA H2A1_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | |||
==About this Structure== | ==About this Structure== | ||
| Line 14: | Line 13: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:012559907</ref><references group="xtra"/> | <ref group="xtra">PMID:012559907</ref><references group="xtra"/><references/> | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Dervan, P B.]] | [[Category: Dervan, P B.]] | ||
Revision as of 04:29, 18 July 2013
LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
Template:ABSTRACT PUBMED 12559907
Function
[H2A1_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [H32_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [H2B11_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
About this Structure
1m18 is a 10 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA.
See Also
Reference
- Suto RK, Edayathumangalam RS, White CL, Melander C, Gottesfeld JM, Dervan PB, Luger K. Crystal structures of nucleosome core particles in complex with minor groove DNA-binding ligands. J Mol Biol. 2003 Feb 14;326(2):371-80. PMID:12559907
