Homology modelling of the core domain of the endogenous lectin comitin: structural basis for its man...
Homology modelling of the core domain of the endogenous lectin comitin: structural basis for its mannose-binding specificity
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Netherlands: Springer Nature B.V
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English
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Netherlands: Springer Nature B.V
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The N-terminal core domain of comitin from the slime mold Dictyostelium discoideum has been modelled from the X-ray coordinates of the monocot mannose-binding lectin from snowdrop (Galanthus nivalis). Docking experiments performed on the three-dimensional model showed that two of the three mannose-binding sites of the comitin monomer are functional...
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Homology modelling of the core domain of the endogenous lectin comitin: structural basis for its mannose-binding specificity
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TN_cdi_proquest_miscellaneous_69778366
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_69778366
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ISSN
0167-4412
E-ISSN
1573-5028
DOI
10.1023/A:1006133527621
