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Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments
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Probert, Fay, Whittaker, S. B.- M, Crispin, Max, Mitchell, Daniel A. and Dixon, Ann M. (2013) Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments. Journal of Biological Chemistry, Volume 288 (Number 31). pp. 22745-22757. doi:10.1074/jbc.M113.458299 ISSN 0021-9258.
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Official URL: http://dx.doi.org/10.1074/jbc.M113.458299
Abstract
Background: DC-SIGNR, a C-type lectin which promotes infection of pathogens such as HIV, is a promising drug target.
Results: Carbohydrate recognition domain of DC-SIGNR is highly dynamic, displaying unique binding modes for individual glycans.
Conclusion: More complex, disease-associated glycans have different binding modes than smaller glycans previously studied.
Significance: Understanding ligand-binding properties and solution dynamics of DC-SIGNR will facilitate therapeutic design
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Research Centres > Molecular Organisation and Assembly in Cells (MOAC) Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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Journal or Publication Title: | Journal of Biological Chemistry | ||||
Publisher: | American Society for Biochemistry and Molecular Biology | ||||
ISSN: | 0021-9258 | ||||
Official Date: | 20 June 2013 | ||||
Dates: |
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Volume: | Volume 288 | ||||
Number: | Number 31 | ||||
Page Range: | pp. 22745-22757 | ||||
DOI: | 10.1074/jbc.M113.458299 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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