Linked Life Data

2682606

Source:http://linkedlifedata.com/resource/pubmed/id/2682606

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1989-12-1
pubmed:abstractText
The amino acid sequence of the central globular domain of histone H1/H5 family members is highly homologous. Twenty-four such sequences have been compared to establish the conserved and variable residues. Fitting this to the tertiary structure of the H5 globular domain shows which of the conserved and variable residues are peripheral and which internal. Particular attention is paid to conserved basic residues on the surface, which we take to be DNA binding. Variable regions and conserved acidic residues are assumed not to be sites of contact with DNA. We conclude that one face of the domain, containing a cluster of basic residues, is the principal DNA binding site whilst two opposing faces, orthogonal to the principal site and also containing conserved basic residues, are subsidiary DNA binding sites. Since the DNA binding surface of the domain covers a full 180 degrees arc, we propose that it contacts a 'cage' of three DNA strands on the 2-fold axis of the chromatosome.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
577-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Binding of the globular domain of linker histones H5/H1 to the nucleosome: a hypothesis.
pubmed:affiliation
Biophysics Laboratory, Portsmouth Polytechnic, UK.
pubmed:publicationType
Journal Article, Comparative Study, Review, Research Support, Non-U.S. Gov't