Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA
The adenovirus proteinase (AVP) uses both an 11-amino acid peptide (pVlc) 1,2 and the viral DNA 1 as cofactors to increase its catalytic rate constant 6000-fold. The crystal structure 3 of an AVP-pVlc complex at 2.6-Å resolution reveals a new protein fold of an enzyme that is the first member of a n...
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| Veröffentlicht in: | Trends in Biochemical Sciences 1997-10, Vol.22 (10), p.393-398 |
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| container_end_page | 398 |
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| container_title | Trends in Biochemical Sciences |
| container_volume | 22 |
| creator | Mangel, Walter F. Toledo, Diana L. Ding, Jianzhong Sweet, Robert M. McGrath, William J. |
| description | The adenovirus proteinase (AVP) uses both an 11-amino acid peptide (pVlc)
1,2 and the viral DNA
1 as cofactors to increase its catalytic rate constant 6000-fold. The crystal structure
3 of an AVP-pVlc complex at 2.6-Å resolution reveals a new protein fold of an enzyme that is the first member of a new class of cysteine proteinases, which arose via convergent evolution. |
| doi_str_mv | 10.1016/S0968-0004(97)01123-7 |
| format | Article |
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| fulltext | fulltext |
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| ispartof | Trends in Biochemical Sciences, 1997-10, Vol.22 (10), p.393-398 |
| issn | 0968-0004 1362-4326 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79382893 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adenoviridae - enzymology Cysteine Endopeptidases - metabolism DNA, Viral - physiology Models, Molecular Protein Structure, Secondary Time Factors |
| title | Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA |
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