Complex of sialoadhesin with a glycopeptide ligand

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Standard

Complex of sialoadhesin with a glycopeptide ligand. / Bukrinsky, Jens T.; St. Hilaire, Phaedria M.; Meldal, Morten; Crocker, Paul R.; Henriksen, Anette.

I: Biochimica et Biophysica Acta - Proteins and Proteomics, Bind 1702, Nr. 2, 01.11.2004, s. 173-179.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Bukrinsky, JT, St. Hilaire, PM, Meldal, M, Crocker, PR & Henriksen, A 2004, 'Complex of sialoadhesin with a glycopeptide ligand', Biochimica et Biophysica Acta - Proteins and Proteomics, bind 1702, nr. 2, s. 173-179. https://doi.org/10.1016/j.bbapap.2004.08.015

APA

Bukrinsky, J. T., St. Hilaire, P. M., Meldal, M., Crocker, P. R., & Henriksen, A. (2004). Complex of sialoadhesin with a glycopeptide ligand. Biochimica et Biophysica Acta - Proteins and Proteomics, 1702(2), 173-179. https://doi.org/10.1016/j.bbapap.2004.08.015

Vancouver

Bukrinsky JT, St. Hilaire PM, Meldal M, Crocker PR, Henriksen A. Complex of sialoadhesin with a glycopeptide ligand. Biochimica et Biophysica Acta - Proteins and Proteomics. 2004 nov. 1;1702(2):173-179. https://doi.org/10.1016/j.bbapap.2004.08.015

Author

Bukrinsky, Jens T. ; St. Hilaire, Phaedria M. ; Meldal, Morten ; Crocker, Paul R. ; Henriksen, Anette. / Complex of sialoadhesin with a glycopeptide ligand. I: Biochimica et Biophysica Acta - Proteins and Proteomics. 2004 ; Bind 1702, Nr. 2. s. 173-179.

Bibtex

@article{0292e573a9e14908acbdb1f55f3dc30d,
title = "Complex of sialoadhesin with a glycopeptide ligand",
abstract = "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.",
keywords = "Ligand complex, Molecular mimicry, Oligosaccharide mimic, Sialoadhesin, Siglec-1, X-ray structure",
author = "Bukrinsky, {Jens T.} and {St. Hilaire}, {Phaedria M.} and Morten Meldal and Crocker, {Paul R.} and Anette Henriksen",
note = "Funding Information: We thank Pia Breddam for outstanding technical assistance in the protein purification step and Dr. Yngve Cerenius for beam line assistance. Dr. Koen M. Halkes is thanked for synthesis of the sialopeptide ligand. This research was supported by the Danish National Research Council (DANSYNC grant) and the Danish National Research Foundation (SPOCC center). Use of the MAXLABII synchrotron was supported by the European Union through the ARI program.",
year = "2004",
month = nov,
day = "1",
doi = "10.1016/j.bbapap.2004.08.015",
language = "English",
volume = "1702",
pages = "173--179",
journal = "B B A - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Complex of sialoadhesin with a glycopeptide ligand

AU - Bukrinsky, Jens T.

AU - St. Hilaire, Phaedria M.

AU - Meldal, Morten

AU - Crocker, Paul R.

AU - Henriksen, Anette

N1 - Funding Information: We thank Pia Breddam for outstanding technical assistance in the protein purification step and Dr. Yngve Cerenius for beam line assistance. Dr. Koen M. Halkes is thanked for synthesis of the sialopeptide ligand. This research was supported by the Danish National Research Council (DANSYNC grant) and the Danish National Research Foundation (SPOCC center). Use of the MAXLABII synchrotron was supported by the European Union through the ARI program.

PY - 2004/11/1

Y1 - 2004/11/1

N2 - 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.

AB - 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.

KW - Ligand complex

KW - Molecular mimicry

KW - Oligosaccharide mimic

KW - Sialoadhesin

KW - Siglec-1

KW - X-ray structure

UR - http://www.scopus.com/inward/record.url?scp=5444227804&partnerID=8YFLogxK

U2 - 10.1016/j.bbapap.2004.08.015

DO - 10.1016/j.bbapap.2004.08.015

M3 - Journal article

C2 - 15488769

AN - SCOPUS:5444227804

VL - 1702

SP - 173

EP - 179

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

SN - 1570-9639

IS - 2

ER -

ID: 327947621