| Title : Crystallization and preliminary X-ray analysis of carboxypeptidase Y inhibitor IC complexed with the cognate proteinase - Mima_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_1622 |
| Author(s) : Mima J , Hayashida M , Fujii T , Hata Y , Hayashi R , Ueda M |
| Ref : Acta Crystallographica D Biol Crystallogr , 60 :1622 , 2004 |
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Abstract :
Carboxypeptidase Y (CPY) inhibitor I(C) is a naturally occurring serine carboxypeptidase inhibitor from Saccharomyces cerevisiae, the sequence of which is not homologous with any other known proteinase inhibitor and is classified as the phosphatidylethanolamine-binding protein (PEBP). I(C) has been crystallized in complex with the deglycosylated form of CPY by the hanging-drop vapour-diffusion technique with ammonium sulfate as a precipitant. The crystals of the complex belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 81.13, b = 186.6, c = 65.14 A. Diffraction data were collected to 2.7 A resolution. Structure determination of the complex is in progress by the molecular-replacement method using the structure of CPY as a search model. |
| PubMedSearch : Mima_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_1622 |
| PubMedID: 15333936 |
| Gene_locus related to this paper: yeast-cbpy1 |
| Gene_locus | yeast-cbpy1 |
| Structure | 1WPX |
Mima J, Hayashida M, Fujii T, Hata Y, Hayashi R, Ueda M (2004)
Crystallization and preliminary X-ray analysis of carboxypeptidase Y inhibitor IC complexed with the cognate proteinase
Acta Crystallographica D Biol Crystallogr
60 :1622
Mima J, Hayashida M, Fujii T, Hata Y, Hayashi R, Ueda M (2004)
Acta Crystallographica D Biol Crystallogr
60 :1622