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Prefoldin beta; Prefoldin is a hexameric molecular chaperone complex, composed of two evolutionarily related subunits (alpha and beta), which are found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The hexameric structure consists of a double beta barrel assembly with six protruding coiled-coils. The alpha prefoldin subunits have two beta hairpin structures while the beta prefoldin subunits (this CD) have only one hairpin that is most similar to the second hairpin of the alpha subunit. The prefoldin hexamer consists of two alpha and four beta subunits and is assembled from the beta hairpins of all six subunits. The alpha subunits initially dimerize providing a structural nucleus for the assembly of the beta subunits. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer.
No pairwise interactions are available for this conserved domain.
Tips:  If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position. The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs. Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below. Range on the Protein: Protein ID Protein Position Domain Position: 
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