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Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin.

Abstract:

The Siglec family of receptors mediates cell-surface interactions through recognition of sialylated glycoconjugates. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. To characterize further the carbohydrate-binding properties, we have determined the crystal structures of SnD1 in the absence of ligand, and in complex with 2-benzyl-Neu5NPro and 2-benzyl-...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2006.10.084

Authors


Journal:
Journal of molecular biology More from this journal
Volume:
365
Issue:
5
Pages:
1469-1479
Publication date:
2007-02-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:11378
UUID:
uuid:686d9d5c-4292-4ef3-ac7d-660c3d855483
Local pid:
pubs:11378
Source identifiers:
11378
Deposit date:
2012-12-19

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