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

Deborah E. Leckband, Sindhu Menon, Kenneth Rosenberg, Sarah A. Graham, Maureen E. Taylor, Kurt Drickamer

Research output: Contribution to journalArticle

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, relatively rigid structure of the neck repeat observed in crystals. In addition, differences in the lengths of DC-SIGN and DC-SIGNR extracellular domains with equivalent numbers of neck repeats support a model in which the different dispositions of the carbohydrate-recognition domains in DC-SIGN and DC-SIGNR result from variations in the sequences of the necks.

Original languageEnglish (US)
Pages (from-to)6125-6132
Number of pages8
JournalBiochemistry
Volume50
Issue number27
DOIs
StatePublished - Jul 12 2011

ASJC Scopus subject areas

  • Biochemistry

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