Glycoproteins generally exist as populations of glycosylated variants (glycoforms) of a single
polypeptide. Although the same glycosylation machinery is available to all proteins that …

The protein-protein interaction underlying l&and recogmtion by CD2 must ensure sprcifuty
while allowing for wry weak binding. The CD5Rbmdmg site on human CD2 has nuw brrn …

Glycosidase inhibitors are moving increasingly out of the laboratory and into the clinic as
potential agents for the treatment of diseases including diabetes, AIDS and cancer. These …

Glycosylation, the addition of sugar residues to a peptide backbone, is the most extensive
posttranslational modification made to proteins by eukaryotic cells. The majority of …

The folding energetics of the mono-N-glycosylated adhesion domain of the human immune
cell receptor cluster of differentiation 2 (hCD2ad) were studied systematically to understand …

The adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution
structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan …

Interaction between CD2 and its counterreceptor, CD58 (LFA-3), on opposing cells
optimizes immune recognition, facilitating contacts between helper T lymphocytes and …

The diversity of the cellular proteome substantially exceeds the number of genes coded by
the DNA of an organism because one or more residues in a majority of eukaryotic proteins …

Considering the small number of papers assessing the conformational profile of
glycoproteins through molecular dynamics (MD) simulations, the current work reports on a …

Rapid progress has recently been made in characterising the structures of leukocyte cell‐
surface molecules. Detailed analyses of the structure and interactions of CD2 were the first …