Sandbox Reserved 642: Difference between revisions

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'''Tetramerization Domain'''  
'''Tetramerization Domain'''  
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' />   
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' />   
'''Regulatory Domain'''
Housed in the N-terminus, the regulatory domain contains residues 19-142 and is more flexible than the other domains. The core of this domain contains an alpha beta sandwich and a beta alpha beta double motif. <ref> Bostjan Kobe, Ian G. Jennings, Colin M. House1, Belinda J. Michell, Kenneth E. Goodwill, Bernard D. Santarsiero, Raymond C. Stevens, Richard G. H. Cotton and Bruce E. Kemp. Nature Structural Biology  6, 442 - 448 (1999), Structural basis of autoregulation of phenylalanine hydroxylase, [http://http://www.nature.com/nsmb/journal/v6/n5/full/nsb0599_442.html]</ref>


== '''Mechanism''' ==
== '''Mechanism''' ==
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