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Journal article

Characterization of the sialic acid-binding site in sialoadhesin by site-directed mutagenesis.

Abstract:

The sialoadhesins are a distinct subgroup of the immunoglobulin superfamily, comprising sialoadhesin, CD22, the myelin-associated glycoprotein, and CD33. They can all mediate sialic acid-dependent binding to cells with distinct specificities. Sialoadhesin is a murine macrophage-restricted cell-surface molecule with 17 extracellular immunoglobulin-like domains that recognizes NeuAc alpha 2-3Gal in N- and O-glycans and interacts preferentially with cells of the granulocytic lineage. Its sialic ...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.271.16.9267

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
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Journal:
The Journal of biological chemistry
Volume:
271
Issue:
16
Pages:
9267-9272
Publication date:
1996-04-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:f6cc859c-e67f-4614-bbae-98932c515bf7
Source identifiers:
29695
Local pid:
pubs:29695

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