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[[Image:1url.gif|left|200px]]<br />
<applet load="1url" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1url, resolution 2.40&Aring;" />
'''N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE'''<br />


==Overview==
==N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE==
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.
<StructureSection load='1url' size='340' side='right'caption='[[1url]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1url]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1URL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIA:L-HISTIDINE+AMIDE'>HIA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1url FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1url OCA], [https://pdbe.org/1url PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1url RCSB], [https://www.ebi.ac.uk/pdbsum/1url PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1url ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SN_MOUSE 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.<ref>PMID:15364954</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ur/1url_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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<ref>PMID:15488769</ref>
1URL is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with SIA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URL OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15488769 15488769]
</div>
<div class="pdbe-citations 1url" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Synthetic construct]]
[[Category: Bukrinsky, J.T.]]
[[Category: Bukrinsky JT]]
[[Category: Crocker, P.R.]]
[[Category: Crocker PR]]
[[Category: Henriksen, A.]]
[[Category: Henriksen A]]
[[Category: Hilaire, P.M.S.]]
[[Category: Hilaire PMS]]
[[Category: Meldal, M.]]
[[Category: Meldal M]]
[[Category: SIA]]
[[Category: cell adhesion]]
[[Category: immunoglobulin domain]]
[[Category: lectin]]
[[Category: molecular mimicry]]
[[Category: oligosaccharide mimics]]
[[Category: sialoadhesin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:24:45 2007''

Latest revision as of 15:55, 13 December 2023

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 Mus musculus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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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