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1Z7S

The crystal structure of coxsackievirus A21

Summary for 1Z7S
Entry DOI10.2210/pdb1z7s/pdb
DescriptorHuman COXSACKIEVIRUS A21, Human coxsackievirus A21, CALCIUM ION, ... (8 entities in total)
Functional Keywordspicornavirus, coxsackievirus, a21, capsid protein, viral protein, icosahedral virus, virus
Biological sourceHuman coxsackievirus A21
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Total number of polymer chains4
Total formula weight97922.45
Authors
Xiao, C.,Bator-Kelly, C.M.,Rieder, E.,Chipman, P.R.,Craig, A.,Kuhn, R.J.,Wimmer, E.,Rossmann, M.G. (deposition date: 2005-03-28, release date: 2005-08-02, Last modification date: 2024-10-16)
Primary citationXiao, C.,Bator-Kelly, C.M.,Rieder, E.,Chipman, P.R.,Craig, A.,Kuhn, R.J.,Wimmer, E.,Rossmann, M.G.
The crystal structure of coxsackievirus a21 and its interaction with icam-1.
Structure, 13:1019-1033, 2005
Cited by
PubMed 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.
PubMed: 16004874
DOI: 10.1016/j.str.2005.04.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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