PDBsum entry 1jew

Virus/receptor

PDB id: 1jew

Contents

Protein chains

120 a.a.* *

269 a.a.* *

256 a.a.* *

238 a.a.* *

55 a.a.* *

* Residue conservation analysis

* C-alpha coords only

PDB id:

1jew

Name:

Virus/receptor

Title:

Cryo-em structure of coxsackievirus b3(m strain) with its cellular receptor, coxsackievirus and adenovirus receptor (car).

Structure:

Coxsackievirus and adenovirus receptor. Chain: r. Fragment: residues 21-140. Synonym: coxsackievirus b-adenovirus receptor, hcar, cvb3 binding protein. Engineered: yes. Coxsackievirus capsid, coat protein vp1. Chain: 1. Fragment: residues 571-851.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: car. Expressed in: mus musculus. Expression_system_taxid: 10090. Expression_system_cell_line: a9 cells. Coxsackievirus b3 (strain woodruff). Organism_taxid: 103904.

Authors:

M.G.Rossmann,Y.He

Key ref:

Y.He et al. (2001). Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor. Nat Struct Biol, 8, 874-878. PubMed id: 11573093 DOI: 10.1038/nsb1001-874

Date:

19-Jun-01 Release date: 03-Oct-01

Protein chain

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

Seq: 365 a.a.

Struc: 120 a.a.

Protein chain

Q66282  (POLG_CXB3W) -  Genome polyprotein from Coxsackievirus B3 (strain Woodruff)

Seq: 2185 a.a.

Struc: 269 a.a.

Protein chain

Q66282  (POLG_CXB3W) -  Genome polyprotein from Coxsackievirus B3 (strain Woodruff)

Seq: 2185 a.a.

Struc: 256 a.a.*

Protein chain

Q66282  (POLG_CXB3W) -  Genome polyprotein from Coxsackievirus B3 (strain Woodruff)

Seq: 2185 a.a.

Struc: 238 a.a.*

Protein chain

Q66282  (POLG_CXB3W) -  Genome polyprotein from Coxsackievirus B3 (strain Woodruff)

Seq: 2185 a.a.

Struc: 55 a.a.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chains 1, 2, 3, 4: E.C.2.7.7.48 - RNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
• Enzyme class 3: Chains 1, 2, 3, 4: E.C.3.4.22.28 - picornain 3C.
• Reaction: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
• Enzyme class 4: Chains 1, 2, 3, 4: E.C.3.4.22.29 - picornain 2A.
• Reaction: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
• Enzyme class 5: Chains 1, 2, 3, 4: E.C.3.6.1.15 - nucleoside-triphosphate phosphatase.
• Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1038/nsb1001-874

Nat Struct Biol 8:874-878 (2001)

PubMed id: 11573093

Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor.

Y.He, P.R.Chipman, J.Howitt, C.M.Bator, M.A.Whitt, T.S.Baker, R.J.Kuhn, C.W.Anderson, P.Freimuth, M.G.Rossmann.

ABSTRACT

Group B coxsackieviruses (CVB) utilize the coxsackievirus-adenovirus receptor (CAR) to recognize host cells. CAR is a membrane protein with two Ig-like extracellular domains (D1 and D2), a transmembrane domain and a cytoplasmic domain. The three-dimensional structure of coxsackievirus B3 (CVB3) in complex with full length human CAR and also with the D1D2 fragment of CAR were determined to approximately 22 A resolution using cryo-electron microscopy (cryo-EM). Pairs of transmembrane domains of CAR associate with each other in a detergent cloud that mimics a cellular plasma membrane. This is the first view of a virus-receptor interaction at this resolution that includes the transmembrane and cytoplasmic portion of the receptor. CAR binds with the distal end of domain D1 in the canyon of CVB3, similar to how other receptor molecules bind to entero- and rhinoviruses. The previously described interface of CAR with the adenovirus knob protein utilizes a side surface of D1.

Selected figure(s)

Figure 2.
Figure 2. Orthogonal stereo views of the C backbone of CAR D1 and D2 (black) fit into the cryo-EM density. Fragments of CVB3 (blue for VP1, green for VP2 and red for VP3) are also shown. a, The south rim of the canyon, formed by VP2, contacts the A and G -strands of domain D1. b, The sugar moieties of the carbohydrate at Asn 108 are depicted in yellow.

Figure 3.
Figure 3. Stereo diagrams of the ICAM-1, PVR and CAR D1 domains. The -strands are labeled A -G. The amino acids identified as being in the virus -receptor interface are indicated by spheres. a, ICAM-1 with HRV14 and HRV16 in blue, and ICAM-1 with coxsackievirus A21 in red; b, PVR with poliovirus in red; and c, CAR with adenovirus knob in blue and CAR with CVB3 in red. d, Schematic diagram of the modes by which CAR (green) binds to CVB3 (red) and adenovirus19 (blue). The suggested membrane curvature is speculative.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2001, 8, 874-878) copyright 2001.

Figures were selected by an automated process.