Structure of a human rhinovirus complexed with its receptor molecule.
AUTOR(ES)
Olson, N H
RESUMO
Cryoelectron microscopy has been used to determine the structure of a virus when complexed with its glycoprotein cellular receptor. Human rhinovirus 16 complexed with the two amino-terminal, immunoglobulin-like domains of the intercellular adhesion molecule 1 shows that the intercellular adhesion molecule 1 binds into the 12-A deep "canyon" on the viral surface. This result confirms the prediction that the viral-receptor attachment site lies in a cavity inaccessible to the host's antibodies. The atomic structures of human rhinovirus 14 and CD4, homologous to human rhinovirus 16 and intercellular adhesion molecule 1, showed excellent correspondence with observed density, thus establishing the virus-receptor interactions.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=45692Documentos Relacionados
- Structure of human rhinovirus complexed with Fab fragments from a neutralizing antibody.
- Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor
- Structure of Adenovirus Complexed with Its Internalization Receptor, αvβ5 Integrin
- Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2.
- Structural Analysis of Human Rhinovirus Complexed with ICAM-1 Reveals the Dynamics of Receptor-Mediated Virus Uncoating