Linked Life Data

17878204

Source:http://linkedlifedata.com/resource/pubmed/id/17878204

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2007-10-31
pubmed:abstractText
We expand the functionally uncharacterized DOMON domain superfamily to identify several novel families, including the first prokaryotic representatives. Using several computational tools we show that it is involved in ligand binding--either as heme- or sugar-binding domains. We present evidence that the DOMON domain along with the DM13 domain comprises a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. Other novel versions might function as sugar sensors of histidine kinases of bacterial two component systems. Supplementary information: Supplementary data are available at Bioinformatics online and also at ftp://ftp.ncbi.nih.gov/pub/aravind/domon/.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1367-4811
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2660-4
pubmed:dateRevised
2009-11-4
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The DOMON domains are involved in heme and sugar recognition.
pubmed:affiliation
National Center for Biotechnology Information, National Library of Medicine and National Institute of Health, Bethesda, MD 20894, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Intramural