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The core of the complex is a house, built in the nineteen-twenties, in which T. E. Lawrence once stayed.
The core of the complex has a ring structure consisting of six proteins that all belong to the same class of RNases, the RNase PH-like proteins.
This system has been studied primarily in the phytopathogen R. solanacearum GMI1000 where it forms the core of the complex network that regulates virulence and pathogenicity genes [60].
The PB1 subunit is the core of the complex and interacts with both PB2 and PA, whereas no interaction between PB2 and PA proteins has been described.
PB1 subunit is the core of the complex and has the polymerase activity [2], [3], and vRNA and cRNA promoter binding activities [4], [5], while PB2 is responsible for cap recognition [6], [7].
The core of the complex is a strong subcomplex between E2 and an E3-binding protein (E3BP).
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Hydrophobic interactions are indicated by the grey region in the core of the complexes and potential ionic interactions are indicated by dashed lines.
In mammalian, yeast and nematode PDC, the E2 (dihydrolipoamide acetyltransferase) together with the E3BP (E3-binding protein) form the complex core [ 1– 5], whereas in plants and bacteria it is E2 alone that generates the core of the PDC complex [ 6– 8].
The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRα in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle.
The core of the cohesin complex comprises four proteins.
The core of the dynein complex is a homodimer of the heavy chains which binds to microtubules and enables cytoplasmic dynein to move in an ATP dependent manner [5], [6].
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