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. 1990 Jan;9(1):9–15. doi: 10.1002/j.1460-2075.1990.tb08074.x

The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution.

M C Lawrence 1, E Suzuki 1, J N Varghese 1, P C Davis 1, A Van Donkelaar 1, P A Tulloch 1, P M Colman 1
PMCID: PMC551622  PMID: 2295315

Abstract

The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.

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Selected References

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