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Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin.

Abstract:

The mode of binding of oligosaccharides to griffithsin, an antiviral lectin from the red alga Griffithsia sp., was investigated by a combination of X-ray crystallography, isothermal titration calorimetry, and molecular modeling. The structures of complexes of griffithsin with 1-->6alpha-mannobiose and with maltose were solved and refined at the resolution of 2.0 and 1.5 A, respectively. The thermodynamic parameters of binding of 1-->6alpha-mannobiose, maltose, and mannose to griffithsin...

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Publication status:
Published

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Publisher copy:
10.1002/prot.21336

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Journal:
Proteins
Volume:
67
Issue:
3
Pages:
661-670
Publication date:
2007-05-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:a00a3dfe-3bd4-41d5-beef-3204fcf827f0
Source identifiers:
100307
Local pid:
pubs:100307

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