Hox protein: Difference between revisions
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===Major Groove Base Readout=== | ===Major Groove Base Readout=== | ||
Hox proteins achieve a large fraction of their binding specificity through <scene name='Sandbox_Reserved_169/Scr_mg/6'>hydrogen bonds between residues of the recognition helix and base pairs in the major groove</scene>. This form of protein-<font color="#e06800">'''DNA'''</font> recognition in the major groove is characterized as '''base readout''' since hydrogen bonds in the major groove can be used to distinguish between all four possible base pairs, A/T, T/A, C/G, and G/C. The Scr residues that engage in major groove base readout are Ile47, Gln50, Asn51, and Met54. Major groove contacts are almost identical across the Hox protein family and are not sufficient to achieve specificity within this family of transcription factors.< | Hox proteins achieve a large fraction of their binding specificity through <scene name='Sandbox_Reserved_169/Scr_mg/6'>hydrogen bonds between residues of the recognition helix and base pairs in the major groove</scene>. This form of protein-<font color="#e06800">'''DNA'''</font> recognition in the major groove is characterized as '''base readout''' since hydrogen bonds in the major groove can be used to distinguish between all four possible base pairs, A/T, T/A, C/G, and G/C. The Scr residues that engage in major groove base readout are Ile47, Gln50, Asn51, and Met54. Major groove contacts are almost identical across the Hox protein family and are not sufficient to achieve specificity within this family of transcription factors. | ||
*<scene name='Sandbox_Reserved_169/Scr_mg/7'>7</scene> | |||
*<scene name='Sandbox_Reserved_169/Scr_mg/8'>8</scene> | |||
===Minor Groove Shape Readout=== | ===Minor Groove Shape Readout=== | ||