Linked Life Data

8178371

Source:http://linkedlifedata.com/resource/pubmed/id/8178371

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-6-9
pubmed:abstractText
The high-mobility group (HMG) domain is a DNA-binding motif that is shared abundant non-histone components of chromatin and by specific regulators of transcription and cell differentiation. The HMG family of proteins comprises members with multiple HMG domains that bind DNA with low sequence specificity, and members with single HMG domains that recognize specific nucleotide sequences. Common properties of HMG domain proteins include interaction with the minor groove of the DNA helix, binding to irregular DNA structures, and the capacity to modulate DNA structure by bending. DNA bending induced by the HMG domain can facilitate the formation of higher-order nucleoprotein complexes, suggesting that HMG domain proteins may have an architectural role in assembling such complexes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0168-9525
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
94-100
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
HMG domain proteins: architectural elements in the assembly of nucleoprotein structures.
pubmed:affiliation
Department of Microbiology, University of California, San Francisco 94143-0414.
pubmed:publicationType
Journal Article, Review