Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4699
|
pubmed:dateCreated |
1985-5-21
|
pubmed:abstractText |
The structure of the (H2A-H2B-H3-H4)2 histone octamer has been determined by means of x-ray crystallographic techniques at a resolution of 3.3 angstroms. The octamer is a prolate ellipsoid 110 angstroms long and 65 to 70 angstroms in diameter, and its general shape is that of a rugby ball. The size and shape are radically different from those determined in earlier studies. The most striking feature of the histone octamer is its tripartite organization, that is, a central (H3-H4)2 tetramer flanked by two H2A-H2B dimers. The DNA helix, placed around the octamer in a path suggested by the features on the surface of the protein, appears like a spring holding the H2A-H2B dimers at either end of the (H3-H4)2 tetramer.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0036-8075
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
3
|
pubmed:volume |
228
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
546-53
|
pubmed:dateRevised |
2007-3-19
|
pubmed:meshHeading |
pubmed-meshheading:3983639-Animals,
pubmed-meshheading:3983639-Chickens,
pubmed-meshheading:3983639-Chromatin,
pubmed-meshheading:3983639-DNA,
pubmed-meshheading:3983639-Histones,
pubmed-meshheading:3983639-Models, Chemical,
pubmed-meshheading:3983639-Nucleosomes,
pubmed-meshheading:3983639-Protein Conformation,
pubmed-meshheading:3983639-X-Ray Diffraction
|
pubmed:year |
1985
|
pubmed:articleTitle |
Crystallographic structure of the octameric histone core of the nucleosome at a resolution of 3.3 A.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|