Sandbox Reserved 642: Difference between revisions

Phenylalanine Hydroxylase exists in equilibrium between a homodimer and a homotetramer.  The region responsible for the tertamerization is the <scene name='Sandbox_Reserved_642/Tetramerization_domain/1'>tetramerization domain</scene> located at the C terminal end of the protein.  It consists of residues 411-452.  The tetramerization domain consists of 2 beta-strands forming a beta-ribbon and an alpha-helix that is 40 angstroms long.  The four alpha helices, consisting of one from each monomer, pack into a coil coil motif with the helices arranged in an anti parallel manner.<ref> Erlandsen H., DirSci; Marianne G. Patch, PhD; Alejandra Gamez, PhD; Mary Straub; and Raymond C. Stevens, PhD. Structural Studies on Phenylalanine Hydroxylase and Implications Toward Understanding and Treating Phenylketonuria [http://www.pkuworld.org/home/docs/literature/erlandsen_2003_p.pdf] <Structure load='1J8U' size='200' frame='true' align='left' caption='catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin' scene='Insert optional scene name here' />