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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Zhou, A. Steiner, D. F. Lipkind, G. M. |
| Description | Author Affiliation: Lipkind GM ( Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.); |
| Abstract | The proprotein convertases are a family of at least seven calcium-dependent endoproteases that process a wide variety of precursor proteins in the secretory pathway. All members of this family possess an N-terminal proregion, a subtilisin-like catalytic module, and an additional downstream well-conserved region of approximately 150 amino acid residues, the P domain, which is not found in any other subtilase. The pro and catalytic domains cannot be expressed in the absence of the P domains; their thermodynamic instability may be attributable to the presence of large numbers of negatively charged Glu and Asp side chains in the substrate binding region for recognition of multibasic residue cleavage sites. Based on secondary structure predictions, we here propose that the P domains consist of 8-stranded beta-barrels with well-organized inner hydrophobic cores, and therefore are independently folded components of the proprotein convertases. We hypothesize further that the P domains are integrated through strong hydrophobic interactions with the catalytic domains, conferring structural stability and regulating the properties and activity of the convertases. A molecular model of these interdomain interactions is proposed in this report. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 13 |
| Volume Number | 95 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1998-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Subtilisins Chemistry Amino Acid Sequence Binding Sites Catalysis Models, Chemical Models, Molecular Molecular Sequence Data Protein Structure, Secondary Sequence Alignment Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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