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Conformational differences in liganded and unliganded states of Galectin-3

Umemoto, K; Leffler, Hakon LU ; Venot, A; Valafar, H and Prestegard, JH (2003) In Biochemistry 42(13). p.3688-3695
Abstract
The conformation of the carbohydrate recognition domain of Galectin-3, a lectin known to bind galactose containing oligosaccharides in mammalian systems, has been investigated in the absence of ligand and in the presence of N-acetylactosamine. A new methodology based on the measurement of residual dipolar couplings from NMR spectra has been used to characterize differences in protein structure along the backbone in the presence and absence of ligand, as well as the binding geometry of the ligand itself. The data on the ligand are consistent with the ligand binding geometry found in a crystal structure of the complexed state. However, a significant rearrangement of backbone loops near the binding site appears to occur in the absence of... (More)
The conformation of the carbohydrate recognition domain of Galectin-3, a lectin known to bind galactose containing oligosaccharides in mammalian systems, has been investigated in the absence of ligand and in the presence of N-acetylactosamine. A new methodology based on the measurement of residual dipolar couplings from NMR spectra has been used to characterize differences in protein structure along the backbone in the presence and absence of ligand, as well as the binding geometry of the ligand itself. The data on the ligand are consistent with the ligand binding geometry found in a crystal structure of the complexed state. However, a significant rearrangement of backbone loops near the binding site appears to occur in the absence of ligand. The implications for ligand specificity and protein functionality are discussed. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
42
issue
13
pages
3688 - 3695
publisher
The American Chemical Society
external identifiers
  • wos:000181996300006
  • pmid:12667058
  • scopus:0344838627
ISSN
0006-2960
DOI
10.1021/bi026671m
language
English
LU publication?
yes
id
9ebc2ae9-d641-4f97-865f-21cde2c862d5 (old id 314997)
date added to LUP
2007-09-23 13:24:23
date last changed
2018-10-03 10:52:41
@article{9ebc2ae9-d641-4f97-865f-21cde2c862d5,
  abstract     = {The conformation of the carbohydrate recognition domain of Galectin-3, a lectin known to bind galactose containing oligosaccharides in mammalian systems, has been investigated in the absence of ligand and in the presence of N-acetylactosamine. A new methodology based on the measurement of residual dipolar couplings from NMR spectra has been used to characterize differences in protein structure along the backbone in the presence and absence of ligand, as well as the binding geometry of the ligand itself. The data on the ligand are consistent with the ligand binding geometry found in a crystal structure of the complexed state. However, a significant rearrangement of backbone loops near the binding site appears to occur in the absence of ligand. The implications for ligand specificity and protein functionality are discussed.},
  author       = {Umemoto, K and Leffler, Hakon and Venot, A and Valafar, H and Prestegard, JH},
  issn         = {0006-2960},
  language     = {eng},
  number       = {13},
  pages        = {3688--3695},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Conformational differences in liganded and unliganded states of Galectin-3},
  url          = {http://dx.doi.org/10.1021/bi026671m},
  volume       = {42},
  year         = {2003},
}