Geometry and adhesion of extracellular domains of DC-SIGNR neck length variants analyzed by force-distance measurements.

ABSTRACT: Force-distance measurements have been used to examine differences in the interaction of the dendritic cell glycan-binding receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR (L-SIGN) with membranes bearing glycan ligands. The results demonstrate that upon binding to membrane-anchored ligand, DC-SIGNR undergoes a conformational change similar to that previously observed for DC-SIGN. The results also validate a model for the extracellular domain of DC-SIGNR derived from crystallographic studies. Force measurements were performed with DC-SIGNR variants that differ in the length of the neck that result from genetic polymorphisms, which encode different numbers of the 23-amino acid repeat sequences that constitute the neck. The findings are consistent with an elongated,

SUBMITTER: Leckband DE 

PROVIDER: S-EPMC3140775 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature