Structural highlights
Function
[GFRP_RAT] Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tetrahydrobiopterin, the cofactor required for hydroxylation of aromatic amino acids regulates its own synthesis in mammals through feedback inhibition of GTP cyclohydrolase I. This mechanism is mediated by a regulatory subunit called GTP cyclohydrolase I feedback regulatory protein (GFRP). The 2.6 A resolution crystal structure of rat GFRP shows that the protein forms a pentamer. This indicates a model for the interaction of mammalian GTP cyclohydrolase I with its regulator, GFRP. Kinetic investigations of human GTP cyclohydrolase I in complex with rat and human GFRP showed similar regulatory effects of both GFRP proteins.
Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP.,Bader G, Schiffmann S, Herrmann A, Fischer M, Gutlich M, Auerbach G, Ploom T, Bacher A, Huber R, Lemm T J Mol Biol. 2001 Oct 5;312(5):1051-7. PMID:11580249[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bader G, Schiffmann S, Herrmann A, Fischer M, Gutlich M, Auerbach G, Ploom T, Bacher A, Huber R, Lemm T. Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP. J Mol Biol. 2001 Oct 5;312(5):1051-7. PMID:11580249 doi:10.1006/jmbi.2001.5011
