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Structural characterisation of ligand-binding determinants in human lung surfactant protein D: influence of Asp325.

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...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2009.09.057

Authors


Shrive, AK More by this author
Paterson, JM More by this author
Martin, JD More by this author
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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

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