 |
PDBsum entry 1rsf
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
1rsf
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Solution structure of the coxsackievirus and adenovirus receptor domain 1.
|
 |
|
Authors
|
 |
S.Jiang,
A.Jacobs,
T.M.Laue,
M.Caffrey.
|
 |
|
Ref.
|
 |
Biochemistry, 2004,
43,
1847-1853.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
|
|
|
 |