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J Mol Biol. 1992 Nov 5;228(1):220-42.

Anatomy and evolution of proteins displaying the viral capsid jellyroll topology.

Author information

1
European Molecular Biology Laboratory, Heidelberg, Germany.

Abstract

In this paper the anatomy of 25 structures containing a jellyroll motif, consisting of eight antiparallel beta-strands forming a so-called beta-barrel, was investigated. This involved performing a careful structural alignment based on hydrogen bonds for the equivalent regions of the tertiary folds and a subsequent analysis of conserved amino acids, equivalenced residue-residue contacts, and various parameters describing the size, shape and other geometrical characteristics of these regions. It was found that the jellyroll motif is best viewed as a two-sheet wedge structure rather than a barrel. The more conserved parameters are discussed. A model of evolutionary development for the jellyroll fold in the various protein and viral structures is proposed.

PMID:
1447783
[Indexed for MEDLINE]

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