Linked Life Data

18844672

Source:http://linkedlifedata.com/resource/pubmed/id/18844672

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-10-10
pubmed:abstractText
The potential mechanisms for driving a ligand to and through a transporter are examined for the leucine transporter using the recently published X-ray structure. Through analyses with computational methods, including investigation of electrostatic properties, site and channel identification, and docking studies, a picture emerges whereby dipolar patches which characterize the electrostatic field serve as the primary driving force to attract the ligand to the protein and begin propagation into it. The electrostatic forces are then augmented by hydrophobic forces in the transport stages, with conformational changes in the protein helping to accommodate the migration. We identify 12 sites that might be involved in ligand recognition and migration. One of these sites corresponds to the tricyclic antidepressant binding site observed in the recently published X-ray structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1747-0285
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-72
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Driving forces for ligand migration in the leucine transporter.
pubmed:affiliation
Department of Computational Chemistry and Structural Biology, H. Lundbeck A/S, 2500 Valby, Denmark.
pubmed:publicationType
Journal Article