Abstract
This review paper aims at discussing the major recent achievements in the field of the heparin-binding proteins (HBPs), primarily chemokines and defensins, and their complexes with glycosaminoglycans examined by solution nuclear magnetic resonance spectroscopy. As opposed to the HBPs involved in coagulation (mainly antithrombin and thrombin), and growth factors (especially fibroblast growth factors 1 and 2), which were extensively analyzed in the past, inflammatory chemokines turned out to be the most thoroughly studied HBPs nowadays. Defensins, which structurally and functionally resemble the chemokines, are also under intensive current investigation.
Keywords: Carbohydrate-protein complex, chemokine, defensin, glycosaminoglycan, heparin, NMR.
Current Protein & Peptide Science
Title:Heparin-Binding Proteins (Chemokines and Defensins) and their Complexes with Glycosaminoglycans from the Solution NMR Perspective
Volume: 15 Issue: 7
Author(s): Vitor H. Pomin
Affiliation:
Keywords: Carbohydrate-protein complex, chemokine, defensin, glycosaminoglycan, heparin, NMR.
Abstract: This review paper aims at discussing the major recent achievements in the field of the heparin-binding proteins (HBPs), primarily chemokines and defensins, and their complexes with glycosaminoglycans examined by solution nuclear magnetic resonance spectroscopy. As opposed to the HBPs involved in coagulation (mainly antithrombin and thrombin), and growth factors (especially fibroblast growth factors 1 and 2), which were extensively analyzed in the past, inflammatory chemokines turned out to be the most thoroughly studied HBPs nowadays. Defensins, which structurally and functionally resemble the chemokines, are also under intensive current investigation.
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Cite this article as:
Pomin H. Vitor, Heparin-Binding Proteins (Chemokines and Defensins) and their Complexes with Glycosaminoglycans from the Solution NMR Perspective, Current Protein & Peptide Science 2014; 15 (7) . https://dx.doi.org/10.2174/138920371507140916145029
DOI https://dx.doi.org/10.2174/138920371507140916145029 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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