2005 journal article

Structure of the conserved transcriptional repressor enhancer of rudimentary homolog

BIOCHEMISTRY, 44(13), 5017–5023.

By: C. Wan n, W. Tempel n, Z. Liu n, B. Wang n & R. Rose n

MeSH headings : Amino Acid Sequence; Animals; Binding Sites; Cell Cycle Proteins / chemistry; Cell Cycle Proteins / genetics; Cell Cycle Proteins / metabolism; Conserved Sequence; Crystallography, X-Ray; Dimerization; Evolution, Molecular; Humans; In Vitro Techniques; Models, Molecular; Molecular Sequence Data; Protein Structure, Quaternary; Protein Structure, Secondary; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Sequence Homology, Amino Acid; Static Electricity; Transcription Factors / chemistry; Transcription Factors / genetics; Transcription Factors / metabolism
TL;DR: Structural and biochemical evidence is presented that erh functions as a dimer, and two putative CKII phosphorylation sites are predicted to disrupt dimerization and protein-protein interactions. (via Semantic Scholar)
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