- Abstract:
-
The crystal structures of a biologically and therapeutically active recombinant homotrimeric fragment of human lung surfactant protein D with a series of bound ligands have been determined. While the structures reveal various different binding modes, all utilise a similarly positioned pair of mannose-type O3' and O4' hydroxyls with no direct interaction between any non-terminal sugar and protein. The orientation, position, and interactions of the bound terminal sugar depend on the sugar itsel...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.jmb.2009.09.057
-
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- Journal:
- Journal of molecular biology
- Volume:
- 394
- Issue:
- 4
- Pages:
- 776-788
- Publication date:
- 2009-12-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:67a0a3c7-c325-4808-828b-7a36a1963f35
- Source identifiers:
-
110078
- Local pid:
- pubs:110078
- Copyright date:
- 2009
Journal article
Structural characterisation of ligand-binding determinants in human lung surfactant protein D: influence of Asp325.
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