Watching One’s P’s and Q’s: Promiscuity, Plasticity, and Quasiequivalence in a T = 1 Virus

Although quasiequivalence is not needed to explain the assembly of the T = 1 canine parvovirus capsid, the interactions of the 60-fold symmetrical capsid protein with less symmetrical viral components illustrate the elements of plasticity and promiscuity of interactions that are embodied in quasiequ...

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Bibliographic Details
Published in:Biophysical journal 1998, Vol.74 (1), p.639-644
Main Author: Chapman, Michael S.
Format: Article
Language:English
Subjects:
ADN
Alternative Splicing
Amino Acid Sequence
Animals
Binding Sites
CANINE PARVOVIRUS
Capsid - biosynthesis
Capsid - chemistry
Capsid - metabolism
COAT PROTEINS
Databases as Topic
DNA
DNA, Viral - metabolism
Dogs
MICROBIAL PROTEINS
Models, Biological
Models, Molecular
Molecular Sequence Data
Parvovirus - physiology
PARVOVIRUS CANIN
PARVOVIRUS CANINO
Protein Structure, Secondary
PROTEINAS MICROBIANAS
PROTEINE MICROBIENNE
RNA, Messenger - metabolism
Virus Assembly
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Summary:Although quasiequivalence is not needed to explain the assembly of the T = 1 canine parvovirus capsid, the interactions of the 60-fold symmetrical capsid protein with less symmetrical viral components illustrate the elements of plasticity and promiscuity of interactions that are embodied in quasiequivalence. The current analysis is based on interactions of fivefold related proteins with a single peptide running along the fivefold axis, and on interactions of the capsid protein with various fragments of the genomic DNA, each having a different sequence and exposing the protein to interactions with different types of nucleotide base.
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(98)77823-3