PDBsum entry 1f5w

Viral protein receptor

PDB id: 1f5w

Contents

Protein chains

124 a.a. *

Ligands

SO4 ×3

Waters ×232

* Residue conservation analysis

PDB id:

1f5w

Name:

Viral protein receptor

Title:

Dimeric structure of the coxsackie virus and adenovirus receptor d1 domain

Structure:

Coxsackie virus and adenovirus receptor. Chain: a, b. Fragment: d1 domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: hela cell cdna library

Biol. unit:

Dimer (from PQS)

Resolution:

1.70Å R-factor: 0.160 R-free: 0.193

Authors:

M.J.Van Raaij,E.Chouin,H.Van Der Zandt,J.M.Bergelson,S.Cusack

Key ref:

M.J.van Raaij et al. (2000). Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution. Structure, 8, 1147-1155. PubMed id: 11080637 DOI: 10.1016/S0969-2126(00)00528-1

Date:

18-Jun-00 Release date: 08-Nov-00

Protein chains

P78310  (CXAR_HUMAN) -  Coxsackievirus and adenovirus receptor from Homo sapiens

Seq: 365 a.a.

Struc: 124 a.a.

DOI no: 10.1016/S0969-2126(00)00528-1

Structure 8:1147-1155 (2000)

PubMed id: 11080637

Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution.

M.J.van Raaij, E.Chouin, H.van der Zandt, J.M.Bergelson, S.Cusack.

ABSTRACT

BACKGROUND: The coxsackievirus and adenovirus receptor (CAR) comprises two extracellular immunoglobulin domains, a transmembrane helix and a C-terminal intracellular domain. The amino-terminal immunoglobulin domain (D1) of CAR is necessary and sufficient for adenovirus binding, whereas the site of coxsackievirus attachment has not yet been localized. The normal cellular role of CAR is currently unknown, although CAR was recently proposed to function as a homophilic cell adhesion molecule. RESULTS: The human CAR D1 domain was bacterially expressed and crystallized. The structure was solved by molecular replacement using the structure of CAR D1 bound to the adenovirus type 12 fiber head and refined to 1.7 A resolution, including individual anisotropic temperature factors. The two CAR D1 structures are virtually identical, apart from the BC, C"D, and FG loops that are involved both in fiber head binding and homodimerization in the crystal. Analytical equilibrium ultracentrifugation shows that a dimer also exists in solution, with a dissociation constant of 16 microM. CONCLUSIONS: The CAR D1 domain forms homodimers in the crystal using the same GFCC'C" surface that interacts with the adenovirus fiber head. The homodimer is very similar to the CD2 D1-CD58 D1 heterodimer. CAR D1 also forms dimers in solution with a dissociation constant typical of other cell adhesion complexes. These results are consistent with reports that CAR may function physiologically as a homophilic cell adhesion molecule in the developing mouse brain. Adenovirus may thus have recruited an existing and conserved interaction surface of CAR to use for its own cell attachment.

Selected figure(s)

Figure 3.
Figure 3. The CAR D1 Homodimer(a) The CAR D1 dimer viewed down the noncrystallographic dyad. Monomer A is colored blue, and B is yellow. Residues involved in direct hydrogen bonds between the two monomers are shown in orange and labeled for monomer A. The N- and C-termini are labeled and the approximate position of the noncrystallographic dyad is indicated.(b) Surface representation of monomer A in blue. The surface that gets buried upon homodimer formation with monomer B is shown in yellow. Residues involved in dimer interactions are indicated. This figure was prepared using the program GRASP [48]

The above figure is reprinted by permission from Cell Press: Structure (2000, 8, 1147-1155) copyright 2000.

Figure was selected by an automated process.