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Literature summary for 3.4.22.15 extracted from

  • Fairhead, M.; Johnson, K.A.; Kowatz, T.; McMahon, S.A.; Carter, L.G.; Oke, M.; Liu, H.; Naismith, J.H.; van der Walle, C.F.
    Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras (2008), Chem. Commun. (Camb. ), 15, 1765-1767.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
chimera C25S/S24A/W26Y/M161L/D162N/G164A/V165M/E159S/D160S/E153S/P154S plus 173ESTESDNN180 to ISNNQ to 1.5 A resolution. Structure is almost identical to cathepsin L Homo sapiens

Protein Variants

Protein Variants Comment Organism
C25S mutant constructed to confer silica condensing activity to cathepsin L. Mutation does not display significant condensing activity Homo sapiens
C25S/S24A/W26Y mutant constructed to confer silica condensing activity to cathepsin L. Mutant displays significant condensing activity Homo sapiens
C25S/S24A/W26Y/M161L/D162N/G164A/V165M mutant constructed to confer silica condensing activity to cathepsin L. Mutant displays significant condensing activity, but less than mutant C25S/S24A/W26Y Homo sapiens
additional information mutant C25S/S24A/W26Y/M161L/D162N/G164A/V165M plus 173ESTESDNN180 to ISNNQ and mutant C25S/S24A/W26Y/M161L/D162N/G164A/V165M/E159S/D160S plus 173ESTESDNN180 to ISNNQ and mutant C25S/S24A/W26Y/M161L/D162N/G164A/V165M/E159S/D160S/E153S/P154S plus 173ESTESDNN180 to ISNNQ increasingly match the features that are unique silicatein alpha. The additional mutations on mutant C25S/S24A/W26Y of cathepsin L to further increase its resemblance to silicatein alpha do not significantly increase the ability to condense silica Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P07711
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