Structural Characterisation of Human Stefin A in Solution and Implications for Binding to Cysteine Proteinases
| Autor: | Vito Turk, L. Kroon-Zitko, Eva Zerovnik, John R. Martin, Jonathan P. Waltho, Roman Jerala |
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| Rok vydání: | 1994 |
| Předmět: |
Magnetic Resonance Spectroscopy
Protein Conformation Proteolysis Molecular Sequence Data Peptide Mapping Biochemistry Protein Structure Secondary Homonuclear molecule Turn (biochemistry) chemistry.chemical_compound medicine Humans Cystatin A Amino Acid Sequence Cystatin B Binding Sites Molecular Structure biology medicine.diagnostic_test Chemistry Electron Spin Resonance Spectroscopy Active site Protein superfamily Cystatins Recombinant Proteins Solutions Cysteine Endopeptidases Papain Heteronuclear molecule Helix biology.protein |
| Zdroj: | European Journal of Biochemistry. 225:1181-1194 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1994.1181b.x |
| Popis: | Stefin A is a member of the cystatin superfamily of proteins which are tight and reversibly binding inhibitors of the papain-like cysteine proteinases. The 'H-NMR and "N-NMR resonances of human stefin A have been sequentially assigned using two-dimensional homonuclear and heteronuclear NMR techniques in conjunction with three-dimensional heteronuclear methods. Characteristic sequential and medium range NOE contacts, J constants and hydrogen exchange data have been used to identify the secondary structural elements of the protein which consists of five anti-parallel P-strands and a single a-helix. There is much similarity between the secondary structural features of stefin A and the homologous protein stefin B in its complex with papain [Stubbs, M. T., Laber, B., Bode, W., Huber, R., Jerala, R., LenarZiE, B. & Turk, V. (1990) EMBO. J. 9, 1939-19471 but also some important differences in regions which are fundamental to the binding event. The principal difference is the presence of two conformationally unrestricted regions in stefin A that form two of the components of the tripartite wedge which docks into the active site of the target proteinase. Specifically, these regions are the five N-terminal residues and the second binding loop, which form a turn and a short helix respectively, in the bound conformation of stefin B. Human stefin A is a member of the cystatin superfamily of proteins, which are tight and reversibly binding inhibitors of the papain-like cysteine proteinases. These inhibitors are believed to help protect cells from inappropriate endogenous or external proteolysis, and are involved in the control mech |
| Databáze: | OpenAIRE |
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