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Comparison of the three‐dimensional structure of two human rhinoviruses (HRV2 and HRV14)
Author(s) -
Blaas Dieter,
Kuechier Ernst,
Vriend Gerrit,
Arnold Edward,
Luo Ming,
Rossmann Michael G.
Publication year - 1987
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340020402
Subject(s) - capsid , amino acid , amino acid residue , peptide sequence , virology , crystallography , biology , virus , chemistry , gene , genetics
An attempt has been made to build a model of human rhinovirus 2 (HRV2) based on the known human rhinovirus 14 (HRV14) structure. HRV2 was selected because its amino acid sequence is known and because it belongs to the minor rhinovirus receptor class as compared to HRV14, which belongs to the major class. Initial alignment of HRV2 with HRV14 based on the primary sequence and the knowlege of the three‐dimensional structure of HRV14 showed that most probable position of the majority of insertions and deletions occurred in the vicinity of the neutralizing immunogenic sites (NIm). Out of a total of 855 amino acids present in one copy of each of the capsid proteins VP1 through VP4 of HRV14, 411 are different between the two viruses. There are also 6 amino acids residues inserted and 14 residues deleted in HRV2 relative to HRV14. Examination of amino acid interactions showed several cases of conservation of function, e.g., salt bridges or the filling of restricted space. The largest variation amongst the residues lining the canyon, the putative receptor binding site, was in the carboxy‐terminal residues of VP1.