1xof
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| , resolution 1.95Å | |||||||
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| Ligands: | , , , | ||||||
| Related: | 1SN9, 1SNA, 1SNE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Heterooligomeric Beta Beta Alpha Miniprotein
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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