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Published online before print June 2, 2006, 10.1110/ps.051994306
Protein Science (2006), 15:1780-1790. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Enhancement of bound-state residual dipolar couplings: Conformational analysis of lactose bound to Galectin-3

Tiandi Zhuang1, Hakon Leffler2 and James H. Prestegard1

1 Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA
2 Section of MIG (Microbiology, Immunology, and Glycobiology), Institute of Laboratory Medicine, Lund University, Lund, Sweden S-223 62

(RECEIVED November 22, 2005; FINAL REVISION March 15, 2006; ACCEPTED March 26, 2006)

Residual dipolar couplings (RDCs) have proven to be a valuable NMR tool that can provide long-range constraints for molecular structure determination. The constraints are orientational in nature and are, thus, highly complementary to conventional distance constraints from NOE data. This complementarity would seem to extend to the study of the geometry of ligands bound to proteins. However, unlike transferred NOEs, where collection, even with a large excess of free ligand, results in measurements dominated by bound contributions, RDCs of exchanging ligands can be dominated by free-state contributions. Here we present a strategy for enhancement of RDCs from bound states that is based on specifically enhancing the alignment of the protein to which a ligand will bind. The protein is modified by addition of a hydrophobic alkyl tail that anchors it to the bicelles that are a part of the ordering medium needed for RDC measurement. As an illustration, we have added a propyl chain to the C terminus of the carbohydrate recognition domain of the protein, Galectin-3, and report enhanced RDCs that prove consistent with known bound-ligand geometries for this protein.

Keywords: RDC; lectin; ligand conformation; NMR; transferred NOE; carbohydrate binding


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T. Zhuang, H.-S. Lee, B. Imperiali, and J. H. Prestegard
Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints
Protein Sci., July 1, 2008; 17(7): 1220 - 1231.
[Abstract] [Full Text] [PDF]


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