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PMID: 18026116 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Structure of the measles virus hemagglutinin.

Nature structural & molecular biology ·Vol. 14 ·No. 12 ·2007-12-00 ·Pages 1227-8

Colf LA, Juo ZS, Garcia KC

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.

MeSH Terms
Binding Sites Hemagglutinins, Viral/chemistry,metabolism Measles virus/chemistry Models, Molecular Protein Conformation
Chemicals
Hemagglutinins, Viral
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Colf Leremy A
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.
Juo Z Sean
Garcia K Christopher
Article Info
Journal
Nature structural & molecular biology
Abbr.
Nat Struct Mol Biol
ISSN
1545-9985
Published
2007-12-00
Epub
2007-00-18
Pages
1227-8
Language
English
Region
United States
NLM ID
101186374
Subset
IM
Databases
PDB
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