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The third protein, Arnt-C/EBP, contains the Arnt basic region and a portion of Helix 1 directly fused to the C/EBP LZ: this hybrid lacks the HLH and PAS domains, so the leucine zipper is the only dimerization element.
The bZIP family shares a basic region and a leucine zipper domain.
Their bHLH domain contains approximately 60 amino acids, including a basic region and a HLH region [ 4].
The bZIP proteins characteristically possess a bZIP domain composed of a basic region and a leucine zipper [ 3].
Plant bZIP proteins characteristically harbor a highly conserved bZIP domain with two structural features: a DNA-binding basic region and a leucine (Leu) zipper dimerization region.
The bZIP trancription factors regulate plant development through a basic region and a leucine zipper dimerization motif that binds to DNA [ 56, 57].
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Members of this family contain a conserved C-terminal basic region and an N-terminal homodimeric parallel coiled coil, which provides a docking site for protein phosphatase 2A's (PP2A) C and B' subunits (Xu et al., 2009).
The Maf protein family belongs to the activator protein 1 (AP-1) superfamily of transcription factors that bind specific DNA target sequences through a basic region and exploit a leucine zipper (LZ) motif for protein protein interactions leading to homo- or hetero-dimerization.
Generally speaking, all of the bHLH transcription factors share a common bHLH motif or domain of approximately 60 amino acids, which contains a basic region and two helices separated by a loop (HLH) region of variable length [ 3– 5, 12].
A cDNA fragment encoding A. fumigatus HapX(24 158) (covering the CBC-binding domain, basic region, and coiled-coil domain) with an extended N-terminus including a cleavage site for tobacco etch virus (TEV) protease was amplified and subcloned into the pMAL-c2X (New England Biolabs) vector.
Group E proteins have Pro or Gly residues within the basic region and can bind preferentially to a typical sequence, CACGNG [ 14].
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