Enhancement of bound-state residual dipolar couplings: Conformational analysis of lactose bound to Galectin-3
(2006) In Protein Science 15(7). p.1780-1790- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/404346
- author
- Zhuang, TD ; Leffler, Hakon LU and Prestegard, JH
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- transferred NOE, NMR, ligand conformation, rDC, lectin, carbohydrate, binding
- in
- Protein Science
- volume
- 15
- issue
- 7
- pages
- 1780 - 1790
- publisher
- The Protein Society
- external identifiers
-
- wos:000238707200020
- pmid:16751604
- scopus:33745698459
- ISSN
- 1469-896X
- DOI
- 10.1110/ps.051994306
- language
- English
- LU publication?
- yes
- id
- 73b1ca68-1601-4abf-8668-ba64a1ca7077 (old id 404346)
- date added to LUP
- 2016-04-01 11:38:58
- date last changed
- 2022-02-10 19:30:08
@article{73b1ca68-1601-4abf-8668-ba64a1ca7077,
abstract = {{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.}},
author = {{Zhuang, TD and Leffler, Hakon and Prestegard, JH}},
issn = {{1469-896X}},
keywords = {{transferred NOE; NMR; ligand conformation; rDC; lectin; carbohydrate; binding}},
language = {{eng}},
number = {{7}},
pages = {{1780--1790}},
publisher = {{The Protein Society}},
series = {{Protein Science}},
title = {{Enhancement of bound-state residual dipolar couplings: Conformational analysis of lactose bound to Galectin-3}},
url = {{http://dx.doi.org/10.1110/ps.051994306}},
doi = {{10.1110/ps.051994306}},
volume = {{15}},
year = {{2006}},
}