1254591-47-3Relevant academic research and scientific papers
Insights into the dynamics and molecular recognition features of glycopeptides by protein receptors: The 3D solution structure of hevein bound to the trisaccharide core of N-glycoproteins
Juan Hernandez-Gay, Jose,Arda, Ana,Eller, Steffen,Mezzato, Stefano,Leeflang, Bas R.,Unverzagt, Carlo,Javier Canada,Jimenez-Barbero, Jesus
, p. 10715 - 10726 (2010)
Protein-carbohydrate interactions are at the heart of a variety of essential molecular recognition events. Hevein, a model lectin related to the superantigen family, recognizes the trisaccharide core of N-glycoproteins (1). A combined approach of NMR spectroscopy and molecular modeling has permitted us to demonstrate that an Asn-linked Man(GlcNAc)2 (2) is bound with even higher affinity than (GlcNAc)3. The molecular recognition process entails conformational selection of only one of the possibilities existing for chitooligosaccharides. The deduced 3D structure of the hevein/2 complex permits the extension of polypeptide chains from the Asn moiety of 2, as well as glycosylation at Man O-3 and Man O-6 of the terminal sugar. Given the ubiquity of the Man(GlcNAc)2 core in all mammalian N-glycoproteins, the basic recognition mode presented herein might be extended to a variety of systems with biomedical importance.
