Solution structure of the coxsackievirus and adenovirus receptor domain 1

Biochemistry. 2004 Feb 24;43(7):1847-53. doi: 10.1021/bi035490x.

Abstract

The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer-dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenoviridae / chemistry*
  • Adenoviridae / metabolism
  • Crystallography, X-Ray
  • Dimerization
  • Enterovirus B, Human / chemistry*
  • Enterovirus B, Human / metabolism
  • Humans
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Virus / chemistry*
  • Receptors, Virus / metabolism
  • Solutions
  • Thermodynamics
  • Ultracentrifugation

Substances

  • Peptide Fragments
  • Receptors, Virus
  • Solutions
  • adenovirus receptor
  • coxsackievirus B receptor

Associated data

  • PDB/1RSF