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. 2000 Dec 18;192(12):1697–1706. doi: 10.1084/jem.192.12.1697

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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The effects of DM on the generation of receptive DR1. (a and b) The effects of DM on the binding of HA_Anchorless peptide to wt and DR1_βG86Y. 2.4 μM DR1_βG86Y (a) and wt (b) were incubated with 100 μM FITC-HA_Anchorless peptide for various times in the absence (○) and presence (▪) of DM (1 μM, 0.15 M citrate phosphate buffer, pH 6.0, at 37°C). The calculated rates for peptide binding to DR1_βG86Y, in the absence and presence of DM, to wtDR1 in the presence of DM, and to the receptive wtDR1, were all very similar and ranged between 0.47 and 0.61 s⁻¹μM⁻¹. (c) The kinetics of HA peptide binding to dissociating DR1–HA_Anchorless complex. 50 μM FITC-HA was incubated with 2.4 μM DR1–AMCA–HA_Anchorless complex (isolated by size-exclusion chromatography, citrate buffer, pH 6.0) for various times at 37°C. The unbound peptides were then removed by Sephadex G-50 spin columns in PBS. Samples were read at two wavelengths of 345 (AMCA) and 514 nm (fluorescein). The dissociation data (▪) were fit to a single exponential decay curve. The HA association (○) data were fit to a single exponential binding curve.

The effects of DM on the generation of receptive DR1. (a and b) The effects of DM on the binding of HA_Anchorless peptide to wt and DR1_βG86Y. 2.4 μM DR1_βG86Y (a) and wt (b) were incubated with 100 μM FITC-HA_Anchorless peptide for various times in the absence (○) and presence (▪) of DM (1 μM, 0.15 M citrate phosphate buffer, pH 6.0, at 37°C). The calculated rates for peptide binding to DR1_βG86Y, in the absence and presence of DM, to wtDR1 in the presence of DM, and to the receptive wtDR1, were all very similar and ranged between 0.47 and 0.61 s⁻¹μM⁻¹. (c) The kinetics of HA peptide binding to dissociating DR1–HA_Anchorless complex. 50 μM FITC-HA was incubated with 2.4 μM DR1–AMCA–HA_Anchorless complex (isolated by size-exclusion chromatography, citrate buffer, pH 6.0) for various times at 37°C. The unbound peptides were then removed by Sephadex G-50 spin columns in PBS. Samples were read at two wavelengths of 345 (AMCA) and 514 nm (fluorescein). The dissociation data (▪) were fit to a single exponential decay curve. The HA association (○) data were fit to a single exponential binding curve.