Talk:MTERF1

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Someone please fix the statement about leucine zippers. MTERFs were originally thought to have leucine zippers but with the 3-D structure solved, it turns out that they have a distinct way of binding DNA... they don't do it by leucine zippers, but by the coordination of 8 separate "mterf" motifs. (I don't have the time to annotate this, so someone please do it). — Preceding unsigned comment added by 72.89.181.220 (talk) 05:40, 21 September 2012 (UTC)
 * whoops... I mean 6 motifs.
 * here is correct description...

Rubinson EH, Eichman BF. Nucleic acid recognition by tandem helical repeats. Curr Opin Struct Biol. 2012 Feb;22(1):101-9.

Protein domains constructed from tandem α-helical repeats have until recently been primarily associated with protein scaffolds or RNA recognition. Recent crystal structures of human mitochondrial termination factor MTERF1 and Bacillus cereus alkylpurine DNA glycosylase AlkD bound to DNA revealed two new superhelical tandem repeat architectures capable of wrapping around the double helix in unique ways. Unlike DNA sequence recognition motifs that rely mainly on major groove read-out, MTERF and ALK motifs locate target sequences and aberrant nucleotides within DNA by resculpting the double-helix through extensive backbone contacts. Comparisons between MTERF and ALK repeats, together with recent advances in ssRNA recognition by Pumilio/FBF (PUF) domains, provide new insights into the fundamental principles of protein-nucleic acid recognition.