title: Structure of the measles virus hemagglutinin.
abstract: Measles virus is a highly pathogenic virus that infects roughly 20 million people per year. We report here the crystal structure of the measles virus hemagglutinin, the surface glycoprotein responsible for the binding of measles virus to its host cell receptors. Although the protein lacks neuraminidase activity, its structure resembles a 'dead' neuraminidase fold, presenting spatially distinct receptor-binding sites for its receptors CD46 and SLAM.
authors.affiliation: Howard Hughes Medical Institute, Departments of Molecular and Cellular Physiology and of Structural Biology, Stanford University School of Medicine, Beckman Building B171, 279 Campus Drive, Stanford, California 94305, USA.
authors.forename: Leremy A
authors.initials: LA
authors.lastname: Colf
authors.forename: Z Sean
authors.initials: ZS
authors.lastname: Juo
authors.forename: K Christopher
authors.initials: KC
authors.lastname: Garcia
mesh_terms: D001665:Binding Sites; D006389:Hemagglutinins, Viral / Q000737:chemistry* / Q000378:metabolism; D008459:Measles virus / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D006389:Hemagglutinins, Viral