1xof
Heterooligomeric Beta Beta Alpha Miniprotein
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| , resolution 1.95Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
The study of short, autonomously folding peptides, or "miniproteins," is important for advancing our understanding of protein stability and folding specificity. Although many examples of synthetic alpha-helical structures are known, relatively few mixed alpha/beta structures have been successfully designed. Only one mixed-secondary structure oligomer, an alpha/beta homotetramer, has been reported thus far. In this report, we use structural analysis and computational design to convert this homotetramer into the smallest known alpha/beta-heterotetramer. Computational screening of many possible sequence/structure combinations led efficiently to the design of short, 21-residue peptides that fold cooperatively and autonomously into a specific complex in solution. A 1.95 A crystal structure reveals how steric complementarity and charge patterning encode heterospecificity. The first- and second-generation heterotetrameric miniproteins described here will be useful as simple models for the analysis of protein-protein interaction specificity and as structural platforms for the further elaboration of folding and function.
About this StructureAbout this Structure
1XOF is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Design of a heterospecific, tetrameric, 21-residue miniprotein with mixed alpha/beta structure., Ali MH, Taylor CM, Grigoryan G, Allen KN, Imperiali B, Keating AE, Structure. 2005 Feb;13(2):225-34. PMID:15698566
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