1pto
From Proteopedia
THE STRUCTURE OF A PERTUSSIS TOXIN-SUGAR COMPLEX AS A MODEL FOR RECEPTOR BINDING
Structural highlights
Function[TOX2_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [TOX4_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [TOX3_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [TOX5_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPertussis toxin is an exotoxin from the bacterium Bordetella pertussis which is important the pathogenesis of whooping cough and the generation of a protective immune response. The diverse biological activities of the toxin depend on its ability to recognize carbohydrate-containing receptors on a wide variety of eukaryotic cells. We present here the crystal structure of pertussis toxin complexed with a soluble oligosaccharide from transferrin. Binding sites for the terminal sialic acid-galactose moiety are revealed on both subunits S2 and S3 of the B-oligomer. Identification of amino acid residues involved in receptor binding will improve the design of genetically inactivated toxins for use in new acellular whooping cough vaccines. Structure of a pertussis toxin-sugar complex as a model for receptor binding.,Stein PE, Boodhoo A, Armstrong GD, Heerze LD, Cockle SA, Klein MH, Read RJ Nat Struct Biol. 1994 Sep;1(9):591-6. PMID:7634099[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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