Linked Life Data

16301309

Source:http://linkedlifedata.com/resource/pubmed/id/16301309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-1-23
pubmed:abstractText
Core and linker histones are the most abundant protein components of chromatin. Even though they lack intrinsic structure, the N-terminal "tail" domains (NTDs) of the core histones and the C-terminal tail domain (CTD) of linker histones bind to many different macromolecular partners while functioning in chromatin. Here we discuss the underlying physicochemical basis for how the histone terminal domains can be disordered and yet specifically recognize and interact with different macromolecules. The relationship between intrinsic disorder and amino acid composition is emphasized. We also discuss the potential structural consequences of acetylation and methylation of lysine residues embedded in intrinsically disordered histone tail domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1853-6
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Intrinsic protein disorder, amino acid composition, and histone terminal domains.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA. Jeffrey.C.Hansen@colostate.edu
pubmed:publicationType
Journal Article, Review