| Autor: |
Kelly CA; Department of Chemistry, 560 Oval Drive, Purdue University, West Lafayette, IN 47907, USA., Laskowski M Jr, Qasim MA |
| Jazyk: |
angličtina |
| Zdroj: |
Protein and peptide letters [Protein Pept Lett] 2005 Jul; Vol. 12 (5), pp. 465-71. |
| DOI: |
10.2174/0929866054395383 |
| Abstrakt: |
In single domain, "standard mechanism" protein inhibitors of serine proteinases, about a dozen residues make contact with the cognate enzyme. The remainder of the molecule, the scaffolding, holds the reactive site region of the inhibitor in a canonical conformation, improves the binding by about six orders of magnitude and protects it from proteolysis. However, the stability and global structure of the scaffolding is irrelevant to inhibition, provided that inhibition is measured much below the melting temperature, Tm. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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