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Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details.

Artikel i vetenskaplig tidskrift
Författare Åsa Holmner
Michael Lebens
Susann Teneberg
Jonas Ångström
Mats Ökvist
Ute Krengel
Publicerad i Structure (London, England : 1993)
Volym 12
Nummer/häfte 9
Sidor 1655-67
ISSN 0969-2126
Publiceringsår 2004
Publicerad vid Institutionen för kemi
Institutionen för medicinsk och fysiologisk kemi
Institutionen för medicinsk mikrobiologi och immunologi
Sidor 1655-67
Språk en
Länkar dx.doi.org/10.1016/j.str.2004.06.02...
Ämnesord Asparagine, metabolism, Bacterial Toxins, chemistry, genetics, metabolism, Binding Sites, Blood Group Antigens, metabolism, Cholera Toxin, chemistry, genetics, metabolism, Crystallography, X-Ray, Drug Design, Enterotoxins, chemistry, genetics, metabolism, Escherichia coli Proteins, chemistry, genetics, metabolism, Glycosphingolipids, chemistry, metabolism, Humans, Models, Molecular, Molecular Sequence Data, Molecular Structure, Oligosaccharides, chemistry, metabolism, Protein Binding, Protein Structure, Tertiary, Protein Subunits, chemistry, genetics, metabolism, Recombinant Fusion Proteins, chemistry, genetics, metabolism, Water, chemistry
Ämneskategorier Medicin och Hälsovetenskap

Sammanfattning

A hybrid between the B subunits of cholera toxin and Escherichia coli heat-labile enterotoxin has been described, which exhibits a novel binding specificity to blood group A and B type 2 determinants. In the present investigation, we have determined the crystal structure of this protein hybrid, termed LCTBK, in complex with the blood group A pentasaccharide GalNAcalpha3(Fucalpha2)Galbeta4(Fucalpha3)GlcNAcbeta, confirming not only the novel binding specificity but also a distinct new oligosaccharide binding site. Binding studies revealed that the new specificity can be ascribed to a single mutation (S4N) introduced into the sequence of Escherichia coli heat-labile enterotoxin. At a resolution of 1.9 A, the new binding site is resolved in excellent detail. Main features include a complex network of water molecules, which is well preserved by the parent toxins, and an unexpectedly modest contribution to binding by the critical residue Asn4, which interacts with the ligand only via a single water molecule.

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