Structural Aspects of Heparan Sulfate Binding to Robo1–Ig1–2
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چکیده
منابع مشابه
Structural diversity of heparan sulfate binding domains in chemokines.
Heparan sulfate (HS) molecules are ubiquitous in animal tissues where they function as ligands that are dramatically involved in the regulation of the proteins they bind. Of these, chemokines are a family of small proteins with many biological functions. Their well-conserved monomeric structure can associate in various oligomeric forms especially in the presence of HS. Application of protein su...
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The isolation, purification and structural characterization of human liver heparan sulfate are described. 1H-NMR spectroscopy demonstrates the purity of this glycosaminoglycan (GAG) and two-dimensional 1H-NMR confirmed that it was heparan sulfate. Enzymatic depolymerization of the isolated heparan sulfate, followed by gradient polyacrylamide gel, confirmed its heparin lyase sensitivity. The con...
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Recombinant mouse endostatin produced by mammalian cells was shown to bind to heparin with a K(d) of 0.3 microM, suggesting that this interaction may play a role in its anti-angiogenic activity. Alanine mutagenesis demonstrated that a major site of four clustered arginines (positions 155, 158, 184 and 270) and a second site (R193, R194) are essential for binding. The same epitopes also particip...
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The functions of heparan sulfate (HS) depend on the expression of structural domains that interact with protein partners. Glycosaminoglycans (GAGs) exhibit a high degree of polydispersity in their composition, chain length, sulfation, acetylation, and epimerization patterns. It is essential for the understanding of GAG biochemistry to produce detailed structural information as a function of spa...
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Alphaviruses are arthropod-borne viruses with wide species ranges and diverse tissue tropisms. The cell surface receptors which allow infection of so many different species and cell types are still incompletely characterized. We show here that the widely expressed glycosaminoglycan heparan sulfate can participate in the binding of Sindbis virus to cells. Enzymatic removal of heparan sulfate or ...
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ژورنال
عنوان ژورنال: ACS Chemical Biology
سال: 2016
ISSN: 1554-8929,1554-8937
DOI: 10.1021/acschembio.6b00692