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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

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
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

Background: DC-SIGNR, a C-type lectin that promotes infection of pathogens such as HIV, is a promising drug target. Results: The carbohydrate recognition domain of DC-SIGNR is highly dynamic, displaying unique binding modes for individual glycans. Conclusion: More complex, disease-associated glycans have binding modes different from those of smaller glycans previously studied. Significance: Understanding ligand-binding properties and solution dynamics of DC-SIGNR will facilitate therapeutic design.

0021-9258
22745-22757
Probert, Fay
268eacad-5a47-481f-9423-5633f8524baf
Whittaker, Sara B M
b6a1e8b8-2db2-4452-a8d7-bc5f8a580b5c
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Mitchell, Daniel A.
d489622a-19e8-43a0-87cd-ba866f5212c2
Dixon, Ann M.
ca9db90f-7704-420a-87e4-665ec1beab1a
Probert, Fay
268eacad-5a47-481f-9423-5633f8524baf
Whittaker, Sara B M
b6a1e8b8-2db2-4452-a8d7-bc5f8a580b5c
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Mitchell, Daniel A.
d489622a-19e8-43a0-87cd-ba866f5212c2
Dixon, Ann M.
ca9db90f-7704-420a-87e4-665ec1beab1a

Probert, Fay, Whittaker, Sara 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. The Journal of Biological Chemistry, 288 (31), 22745-22757. (doi:10.1074/jbc.M113.458299).

Record type: Article

Abstract

Background: DC-SIGNR, a C-type lectin that promotes infection of pathogens such as HIV, is a promising drug target. Results: The carbohydrate recognition domain of DC-SIGNR is highly dynamic, displaying unique binding modes for individual glycans. Conclusion: More complex, disease-associated glycans have binding modes different from those of smaller glycans previously studied. Significance: Understanding ligand-binding properties and solution dynamics of DC-SIGNR will facilitate therapeutic design.

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e-pub ahead of print date: 20 June 2013
Published date: 2 August 2013
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Identifiers

Local EPrints ID: 414421
URI: http://eprints.soton.ac.uk/id/eprint/414421
DOI: doi:10.1074/jbc.M113.458299
ISSN: 0021-9258
PURE UUID: 0f512075-9ddb-41dd-844b-6581d0a7ced5
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 28 Sep 2017 16:31
Last modified: 16 Mar 2024 04:30

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Contributors

Author: Fay Probert
Author: Sara B M Whittaker
Author: Max Crispin ORCID iD
Author: Daniel A. Mitchell
Author: Ann M. Dixon

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