Sandbox Reserved 1734: Difference between revisions
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Secondary Structure: | Secondary Structure: | ||
PAH contains right-handed alpha helices and antiparallel beta-strands in its secondary structure. There are some amino acids that don't have any secondary structure, and these are found in the loop containing regions. The loop containing regions are residues L42-V45, D59-H69, S70-D75, and H82-V90. | PAH contains right-handed alpha helices and antiparallel beta-strands in its secondary structure. There are some amino acids that don't have any secondary structure, and these are found in the loop containing regions. The loop containing regions are residues L42-V45, D59-H69, S70-D75, and H82-V90. | ||
Tertiary Structure: | Tertiary Structure: | ||
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Quaternary Structure: | Quaternary Structure: | ||
The quaternary structure of PAH is a homotetramer, dimer of dimers. It is a multidomain, homo-oligomeric protein with dihedral (D2) symmetry. | The quaternary structure of PAH is a homotetramer, dimer of dimers. It is a multidomain, homo-oligomeric protein with dihedral (D2) symmetry. | ||
<Structure load='2PHM' size='250' frame='true' align='left' caption='Human Tetramer' scene='Insert optional scene name here' /> | |||
The substrate of phenylalanine hydroxylase is the amino acid L-phenylalanine. Phenylalanine binds between the regulatory domain and the interacting catalytic domain, near the sequence binding motif. The activation of PAH by L-phenylalanine induces a large conformational change, but a slow global conformational change (is it large in magnitude but slow overall?) Full activation of PAH involves the shift and dimerization of the regulatory domains. | The substrate of phenylalanine hydroxylase is the amino acid L-phenylalanine. Phenylalanine binds between the regulatory domain and the interacting catalytic domain, near the sequence binding motif. The activation of PAH by L-phenylalanine induces a large conformational change, but a slow global conformational change (is it large in magnitude but slow overall?) Full activation of PAH involves the shift and dimerization of the regulatory domains. | ||
