PDBsum entry 1z7z

Virus/receptor

PDB id: 1z7z

Contents

Protein chains

214 a.a. *

263 a.a. *

192 a.a. *

12 a.a. *

434 a.a. *

Ligands

LEU-ILE-GLY-ARG-THR

NAG ×8

* Residue conservation analysis

PDB id:

1z7z

Name:

Virus/receptor

Title:

Cryo-em structure of human coxsackievirus a21 complexed with five domain icam-1kilifi

Structure:

Human coxsackievirus a21. Chain: 1. Fragment: viral protein 1 residues 1073-1286. Human coxsackievirus a21. Chain: 2. Fragment: viral protein 2 residues 2010-2272. Human coxsackievirus a21. Chain: 3. Fragment: viral protein 3 residues 3043-3234.

Source:

Human coxsackievirus a21. Organism_taxid: 12069. Strain: kuykendall. Cell_line: hela. Other_details: the nature host of this virus is human. Homo sapiens. Human. Organism_taxid: 9606. Cell_line: cos7

Authors:

C.Xiao,C.M.Bator-Kelly,E.Rieder,P.R.Chipman,A.Craig,R.J.Kuhn, E.Wimmer,M.G.Rossmann

Key ref:

C.Xiao et al. (2005). The crystal structure of coxsackievirus A21 and its interaction with ICAM-1. Structure, 13, 1019-1033. PubMed id: 16004874 DOI: 10.1016/j.str.2005.04.011

Date:

28-Mar-05 Release date: 02-Aug-05

Protein chain

Q7T7N6  (Q7T7N6_9ENTO) -  Genome polyprotein from Coxsackievirus A21

Seq: 2207 a.a.

Struc: 214 a.a.

Protein chain

Q7T7N6  (Q7T7N6_9ENTO) -  Genome polyprotein from Coxsackievirus A21

Seq: 2207 a.a.

Struc: 263 a.a.

Protein chain

Q7T7N6  (Q7T7N6_9ENTO) -  Genome polyprotein from Coxsackievirus A21

Seq: 2207 a.a.

Struc: 192 a.a.

Protein chain

P22055  (POLG_CXA21) -  Genome polyprotein from Coxsackievirus A21 (strain Coe)

Seq: 2206 a.a.

Struc: 12 a.a.*

Protein chain

P05362  (ICAM1_HUMAN) -  Intercellular adhesion molecule 1 from Homo sapiens

Seq: 532 a.a.

Struc: 434 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: 10.1016/j.str.2005.04.011

Structure 13:1019-1033 (2005)

PubMed id: 16004874

The crystal structure of coxsackievirus A21 and its interaction with ICAM-1.

C.Xiao, C.M.Bator-Kelly, E.Rieder, P.R.Chipman, A.Craig, R.J.Kuhn, E.Wimmer, M.G.Rossmann.

ABSTRACT

CVA21 and polioviruses both belong to the Enterovirus genus in the family of Picornaviridae, whereas rhinoviruses form a distinct picornavirus genus. Nevertheless, CVA21 and the major group of human rhinoviruses recognize intercellular adhesion molecule-1 (ICAM-1) as their cellular receptor, whereas polioviruses use poliovirus receptor. The crystal structure of CVA21 has been determined to 3.2 A resolution. Its structure has greater similarity to poliovirus structures than to other known picornavirus structures. Cryo-electron microscopy (cryo-EM) was used to determine an 8.0 A resolution structure of CVA21 complexed with an ICAM-1 variant, ICAM-1(Kilifi). The cryo-EM map was fitted with the crystal structures of ICAM-1 and CVA21. Significant differences in the structure of CVA21 with respect to the poliovirus structures account for the inability of ICAM-1 to bind polioviruses. The interface between CVA21 and ICAM-1 has shape and electrostatic complementarity with many residues being conserved among those CVAs that bind ICAM-1.

Selected figure(s)

Figure 6.
Figure 6. Road Maps of the ICAM-1^Kilifi Contact Area with CVA21
(A) Stereo diagram of enlarged contact area in Figure 5A.
(B) The viral (left) and ICAM-1^Kilifi (right) residues that are in the virus/receptor interface are shown on a two-dimensional projection of the same contact area (orange) as in (A). The three contour lines represent virus-receptor separation distances of 2.0 (red), 3.0 (orange), and 4.0 (yellow) Å.
(C) Stereo diagram of the contact area (white) with surface color based on electrostatic potentials. Positively and negatively charged surfaces are colored blue and red, respectively.
(D) Two-dimensional projection of (C) with a roadmap of corresponding residues of CVA21 (left) and ICAM-1^Kilifi (right). The four ionic network sites are encircled with green dashed lines and are labeled with green-colored letters of a, b, c, and d, corresponding to the notation used in Figure 7.

The above figure is reprinted by permission from Cell Press: Structure (2005, 13, 1019-1033) copyright 2005.

Figure was selected by an automated process.