Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Structure of SARS coronavirus spike receptor-binding domain complexed with receptor

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Li, F.
  • Li, W. H.
  • Farzan, Michael
  • Harrison, S. C.

publication date

  • September 2005

journal

  • Science  Journal

abstract

  • The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.

subject areas

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Antibodies, Viral
  • Binding Sites
  • Carboxypeptidases
  • Cell Line
  • Crystallography, X-Ray
  • Disease Outbreaks
  • Epitopes
  • Glycosylation
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Membrane Glycoproteins
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Peptidyl-Dipeptidase A
  • Protein Conformation
  • Protein Structure, Tertiary
  • Receptors, Virus
  • SARS Virus
  • Severe Acute Respiratory Syndrome
  • Species Specificity
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins
  • Viral Vaccines
  • Viverridae
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1116480

PubMed ID

  • 16166518
scroll to property group menus

Additional Document Info

start page

  • 1864

end page

  • 1868

volume

  • 309

issue

  • 5742

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support