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~~'''~~N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE~~'''~~

===N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE===

~~==Overview==~~

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~~Sialoadhesin is a sialic acid~~-~~binding immunoglobulin~~-~~like lectin~~ (~~Siglec), expressed~~ on ~~subsets of macrophages~~. ~~It is a model system for Siglec receptor-mediated cell surface interactions through binding of sialylated glycoconjugates~~. ~~The N-terminal sialoadhesin domain can mediate sialic acid-binding on its own. The structure of this domain has been determined in complex with a sialic acid-containing heptapeptide~~, ~~(Ala-Gly-His-Thr(Neu5Ac)-Trp-Gly-His). The affinity of sialoadhesin for this ligand~~ is ~~four times higher than~~ the ~~affinity for the natural linkage 2,3'~~-~~sialyllactose. The structure of the glycopeptide complex suggests strategies for ligand optimization and provides possible explanations for the observed differences in specificities among the Siglecs.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15488769}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15488769 is the PubMed ID number.

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==About this Structure==

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[[Category: Oligosaccharide mimic]]

[[Category: Sialoadhesin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3~~ 11:35:36 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:52:31 2008''

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-[[Image:1url.gif|left|200px]]
+{{Seed}}
+[[Image:1url.png|left|200px]]
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 {{STRUCTURE_1url|  PDB=1url  |  SCENE=  }}
-'''N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE'''
+===N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE===
-==Overview==
+<!--
-Sialoadhesin is a sialic acid-binding immunoglobulin-like lectin (Siglec), expressed on subsets of macrophages. It is a model system for Siglec receptor-mediated cell surface interactions through binding of sialylated glycoconjugates. The N-terminal sialoadhesin domain can mediate sialic acid-binding on its own. The structure of this domain has been determined in complex with a sialic acid-containing heptapeptide, (Ala-Gly-His-Thr(Neu5Ac)-Trp-Gly-His). The affinity of sialoadhesin for this ligand is four times higher than the affinity for the natural linkage 2,3'-sialyllactose. The structure of the glycopeptide complex suggests strategies for ligand optimization and provides possible explanations for the observed differences in specificities among the Siglecs.
+The line below this paragraph, {{ABSTRACT_PUBMED_15488769}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15488769 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15488769}}
 ==About this Structure==
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 [[Category: Oligosaccharide mimic]]
 [[Category: Sialoadhesin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:35:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:52:31 2008''