1url
From Proteopedia
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|PDB= 1url |SIZE=350|CAPTION= <scene name='initialview01'>1url</scene>, resolution 2.40Å | |PDB= 1url |SIZE=350|CAPTION= <scene name='initialview01'>1url</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=AC1:Sia+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Sia+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SIA:O-SIALIC ACID'>SIA</scene> | + | |LIGAND= <scene name='pdbligand=HIA:L-HISTIDINE+AMIDE'>HIA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1url FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1url OCA], [http://www.ebi.ac.uk/pdbsum/1url PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1url RCSB]</span> | ||
}} | }} | ||
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[[Category: Hilaire, P M.S.]] | [[Category: Hilaire, P M.S.]] | ||
[[Category: Meldal, M.]] | [[Category: Meldal, M.]] | ||
| - | [[Category: SIA]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: immunoglobulin domain]] | [[Category: immunoglobulin domain]] | ||
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[[Category: sialoadhesin]] | [[Category: sialoadhesin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:12 2008'' |
Revision as of 21:14, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1URL is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
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