Adodecameric protein has a quaternary structure consisting of 12 protein subunits in a complex. Dodecameric complexes can have a number of subunit 'topologies', but typically only a few of the theoretically possible subunit arrangements are observed in protein structures.
Adodecamer (protein) is a protein complex with 12 protein subunits.
A common subunit arrangement involves a tetrahedral distribution of subunit trimers (or 3-4-point symmetry). Another observed arrangement of subunits puts two rings of six subunits side by side along the sixfold axis (or 2-6-point symmetry).
When multiple copies of a polypeptide encoded by a gene form an aggregate, this protein structure is referred to as a multimer. When a multimer is formed from polypeptides produced by two different mutant alleles of a particular gene, the mixed multimer may exhibit greater functional activity than the unmixed multimers formed by each of the mutants alone. In such a case, the phenomenon is referred to as intragenic complementation or interallelic complementation.[1]
Propionyl-CoA carboxylase (PCC) is a dodecameric heteropolymer composed of α and β subunits in a α6β6 structure. Mutations in PCC, either in the α subunit (PCCα) or β subunit (PCCβ) can cause propionic acidemia in humans. When different mutant skin fibroblast cell lines defective in PCCβ were fused in pairwise combinations, the β heteromultimeric protein formed as a result often exhibited a higher level of activity than would be expected based on the activities of the parental enzymes.[2] This finding of intragenic complementation indicated that the multimeric dodecameric structure of PCC allows cooperative interactions between the constituent PCCβ monomers that can generate a more functional form of the holoenzyme.
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