Linked Life Data

11798029

Source:http://linkedlifedata.com/resource/pubmed/id/11798029

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-5
pubmed:dateCreated
2002-1-18
pubmed:abstractText
The uncoupling protein UCP1 is a member of a superfamily of homologous proteins formed by the mitochondrial metabolite transporters. Although they act in vivo as carriers, under specific experimental conditions some of these transporters have been shown to behave as channels. This dual transport operation suggests that these carriers are likely to be formed by two differentiated functional and structural domains. The kinetic model termed "single binding center gated pore" is well suited to understand the behaviour of these carriers. It proposes that in the protein core there must exist a hydrophilic translocation pore whose access is controlled by gates. It is highly likely that the hydrophilic channel is formed by the transmembrane alpha-helices and that loops contribute to the formation of the gates. UCP1 is regulated physiologically by fatty acids and purine nucleotides. Nucleotides maintain the proton conductance inhibited while fatty acids act as cytosolic second messengers of noradrenaline to active UCP1. Based on photoaffinity labeling and mutagenesis data, we propose a structural model for the localization of the binding site. The nucleotide enters through a gate in the cytosolic side and binds deep inside the protein. The three matrix loops contribute to the formation of a hydrophobic binding pocket that would accommodate the purine moiety. Three arginine residues (in helices II, IV, and VI) would interact with the phosphate groups. His214 and Glu190 have been involved in the pH regulation of the nucleotide binding but because they are on the cytosolic side of the protein, we propose that their state of protonation will determine the access of the nucleotide to the binding center.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1521-6543
pubmed:author
pubmed:issnType
Print
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
The mitochondrial uncoupling protein UCP1: a gated pore.
pubmed:affiliation
MRC-Dunn Human Nutrition Unit, Cambridge, United Kingdom.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't