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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1url ConSurf].
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Revision as of 11:42, 9 February 2016

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

Structural highlights

1url is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SN_MOUSE] Acts as an endocytic receptor mediating clathrin dependent endocytosis. Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells (By similarity). Preferentially binds to alpha-2,3-linked sialic acid. Binds to SPN/CD43 on T-cells. May play a role in hematopoiesis. May act as a counter-receptor for CLEC10A in lymph node.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Complex of sialoadhesin with a glycopeptide ligand.,Bukrinsky JT, St Hilaire PM, Meldal M, Crocker PR, Henriksen A Biochim Biophys Acta. 2004 Nov 1;1702(2):173-9. PMID:15488769[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Kumamoto Y, Higashi N, Denda-Nagai K, Tsuiji M, Sato K, Crocker PR, Irimura T. Identification of sialoadhesin as a dominant lymph node counter-receptor for mouse macrophage galactose-type C-type lectin 1. J Biol Chem. 2004 Nov 19;279(47):49274-80. Epub 2004 Sep 13. PMID:15364954 doi:http://dx.doi.org/10.1074/jbc.M409300200
  2. ↑ Bukrinsky JT, St Hilaire PM, Meldal M, Crocker PR, Henriksen A. Complex of sialoadhesin with a glycopeptide ligand. Biochim Biophys Acta. 2004 Nov 1;1702(2):173-9. PMID:15488769 doi:10.1016/j.bbapap.2004.08.015

1url, resolution 2.40Å

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