title: 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, 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.
authors.affiliation: Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
authors.forename: Deborah E
authors.initials: DE
authors.lastname: Leckband
authors.forename: Sindhu
authors.initials: S
authors.lastname: Menon
authors.forename: Kenneth
authors.initials: K
authors.lastname: Rosenberg
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Graham
authors.forename: Maureen E
authors.initials: ME
authors.lastname: Taylor
authors.forename: Kurt
authors.initials: K
authors.lastname: Drickamer
mesh_terms: D020816:Amino Acid Motifs; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000378:metabolism; D004548:Elasticity; D005110:Extracellular Space / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007368:Interferometry / Q000379:methods; D037181:Lectins, C-Type / Q000737:chemistry* / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D025941:Protein Interaction Mapping / Q000379:methods*; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism; D020449:Repetitive Sequences, Amino Acid; D020349:Surface Plasmon Resonance / Q000379:methods; D013499:Surface Properties; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
chemical_list: D015815:Cell Adhesion Molecules; D037181:Lectins, C-Type; D008051:Lipid Bilayers; D011956:Receptors, Cell Surface; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin; C433029:CLEC4M protein, human