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 language | English (US) |
|---|---|
| Pages (from-to) | 6125-6132 |
| Number of pages | 8 |
| Journal | Biochemistry |
| Volume | 50 |
| Issue number | 27 |
| DOIs | |
| State | Published - Jul 12 2011 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Geometry and adhesion of extracellular domains of DC-SIGNR neck length variants analyzed by force-distance measurements. / Leckband, Deborah E.; Menon, Sindhu; Rosenberg, Kenneth; Graham, Sarah A.; Taylor, Maureen E.; Drickamer, Kurt.
In: Biochemistry, Vol. 50, No. 27, 12.07.2011, p. 6125-6132.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Geometry and adhesion of extracellular domains of DC-SIGNR neck length variants analyzed by force-distance measurements
AU - Leckband, Deborah E.
AU - Menon, Sindhu
AU - Rosenberg, Kenneth
AU - Graham, Sarah A.
AU - Taylor, Maureen E.
AU - Drickamer, Kurt
PY - 2011/7/12
Y1 - 2011/7/12
N2 - 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.
AB - 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.
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U2 - 10.1021/bi2003444
DO - 10.1021/bi2003444
M3 - Article
C2 - 21650186
AN - SCOPUS:79959944073
VL - 50
SP - 6125
EP - 6132
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 27
ER -