Linked Life Data

19492862

Source:http://linkedlifedata.com/resource/pubmed/id/19492862

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-6-4
pubmed:abstractText
Galectins belong to the family of glycan-binding proteins, defined by at least one conserved carbohydrate-recognition domain with a highly conserved amino acid sequence and affinity for beta galactosides. They all possess a tryptophan residue in the carbohydrate binding site that forms hydrophobic contacts with the carbohydrate ligands. Site directed mutagenesis experiments have shown that this conserved aromatic residue plays a key role in the interaction. We have studied the interaction between the corresponding human Galectin-1 in silico mutants and different carbohydrate ligands using molecular dynamics in explicit solvent. The results confirm the importance of the conserved tryptophan residue in the affinity of the ligand and gives further insights into the mode of interaction between lactose derivatives and human Galectin-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0739-1102
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-58
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Computational studies of human galectin-1: role of conserved tryptophan residue in stacking interaction with carbohydrate ligands.
pubmed:affiliation
Unite Interactions et Modulateurs de Reponses, Institut Mediterranen de Microbiologie, CNRS, 31 chemin Joseph Aiguier, Marseille Cedex 20, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't