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DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition

DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4056191

DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition

About this item

Full title

DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2012-11, Vol.491 (7425), p.560-565

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Histone chaperones represent a structurally and functionally diverse family of histone-binding proteins that prevent promiscuous interactions of histones before their assembly into chromatin. DAXX is a metazoan histone chaperone specific to the evolutionarily conserved histone variant H3.3. Here we report the crystal structures of the DAXX histone-...

Alternative Titles

Full title

DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4056191

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4056191

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature11608