Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1990-11-15
pubmed:abstractText
We describe herein the high resolution refined x-ray structure of a trisaccharide, which is a part of the N-acetyllactosamine type glycan found in the majority of the N-glycosyl-proteins, complexed to the isolectin I. According to the potentials used by Imberty et al. (Imburty, A., Gerber, S., Tran, V., and Pérez, S. (1990) Glycoconjugate J. 7, 27-54) the trisaccharide is in a low-energy state. Only one mannose moiety establishes direct hydrogen bonds with the lectin, as it is the case for monosaccharide-lectin complexes. The comparison of our trisaccharide with the one determined in solution by Warin et al. (Warin, V., Baert, F., Fouret, R., Strecker, G., Fournet, B., and Montreuil, J. (1979) Carbohydr. Res. 76, 11-22) shows that both adopt roughly the same conformation. The differences in these two sugar structures allow us to assign the role of water molecules present in the vicinity of our trisaccharide for the stabilization of this sugar-lectin complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18161-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
X-ray structure of a (alpha-Man(1-3)beta-Man(1-4)GlcNAc)-lectin complex at 2.1-A resolution. The role of water in sugar-lectin interaction.
pubmed:affiliation
Laboratoire de Cristallographie et de Cristallisation des Macromolécules Biologiques, Faculté de Médecine, Marseille, France.
pubmed:publicationType
Journal Article