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Literature summary for 3.4.21.75 extracted from
- Conformational analyses of a partially-folded bioactive prodomain of human furin (2007), Biopolymers, 86, 329-344.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | in the presence of trifluoroethanol, the N-terminal half of the prodomain is better structured and more compactly folded than the C-terminal half of the prodomain. N-terminal residues 1-46 of the prodomain in 50% trifluoroethanol populates backbone conformations containing a short helix, a beta-strand and a helix-loop-helix supersecondary structure with elements of tertiary interactions. The intervening segment (residues 47-65) is predominately unstructured with a long and highly flexible region surrounding the protease activation loop followed by a partially helical segment in the C-terminal end. A peptide fragment derived from residues Pro16-Arg49 can form the helix-loop-helix structure in aqueous solution in the absence of trifluoroethanol | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| full-length furin prodomain overexpressed in Escherichia coli strain BL21 (DE3) | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the prodomain exhibits inhibitory action toward furin | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by Ni2+ affinity chromatography | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Proprotein convertase | - |
Homo sapiens |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
a positively-charged Lys residue replacing His43 in the 16-49 fragment imparts stability to the super-secondary structure of the furin prodomain at both acidic and neutral pH | Homo sapiens |
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Release 2023.1 (January 2023)
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