1Z7Z
Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi
Summary for 1Z7Z
Entry DOI | 10.2210/pdb1z7z/pdb |
Related | 1IAM 1Z7S |
EMDB information | 1114 |
Descriptor | human coxsackievirus A21, Intercellular adhesion molecule-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
Functional Keywords | icam-1, kilifi, cd54, human coxsackievirus a21, virus-receptor complex, icosahedral virus, virus/receptor |
Biological source | Human coxsackievirus A21 More |
Total number of polymer chains | 6 |
Total formula weight | 140661.67 |
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: 2021-10-20) |
Primary citation | Xiao, 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: 16004874DOI: 10.1016/j.str.2005.04.011 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8 Å) |
Structure validation
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