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PMID: 3612789 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus.

Journal of molecular biology ·Vol. 193 ·No. 4 ·1987-02-20 ·Pages 693-707

Altschuh D, Lesk AM, Bloomer AC, Klug A

Abstract

Sequence data are available for the coat proteins of seven tobamoviruses, with homologies ranging from at least 26% to 82%, and atomic co-ordinates are known for tobacco mosaic virus (TMV) vulgare. A significant spatial relationship has been found between groups of residues with identical amino acid substitution patterns. This strongly suggest that their location is linked to a particular function, at least in viruses identical with the wild-type for these residues. The most conserved feature of TMV is the RNA binding region. Core residues are conserved in all viruses or show mutations complementary in volume. The specificity of inter-subunit contacts is achieved in different ways in the three more distantly related viruses.

MeSH Terms
Amino Acid Sequence Binding Sites Protein Conformation RNA, Viral Tobacco Mosaic Virus/analysis,classification Viral Proteins/classification
Chemicals
RNA, Viral Viral Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Altschuh D
Lesk A M
Bloomer A C
Klug A
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1987-02-20
Pages
693-707
Language
English
Region
England
NLM ID
2985088R
Subset
IM
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