| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8290909 | Archives of Biochemistry and Biophysics | 2013 | 10 Pages |
Abstract
⺠A new morpheein model for PAH allostery is proposed: 4merâ â 2merâ â 2mer â 4mer. ⺠Protein structure models are presented for low activity 4merâ and Phe activated 4mer. ⺠Mammalian PAH is shown to consist of an equilibrium of architecturally distinct multimers. ⺠Spectroscopic, chromatographic, and kinetic data support the proposed models. ⺠This work holds promise for developing allosteric pharmacologic chaperones to treat PKU.
Keywords
PAH3-deoxy-d-arabino-heptulosonate 7-phosphate synthaseProtein homology modelingDAH7PSPBGstetrahydrobiopterinBH4PAGEPKUPHEPDBMBPSECSDSphenylketonuriapolyacrylamide gel electrophoresissodium dodecyl sulfatePharmacological chaperonePhenylalanine hydroxylasePhenylalanineProtein Data Bankmaltose binding proteinPorphobilinogen synthaseSize exclusion chromatographyIon exchange chromatographyIEC
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Authors
Eileen K. Jaffe, Linda Stith, Sarah H. Lawrence, Mark Andrake, Roland L. Jr.,