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Literature summary for 3.4.21.B6 extracted from

  • Spraggon, G.; Hornsby, M.; Shipway, A.; Tully, D.C.; Bursulaya, B.; Danahay, H.; Harris, J.L.; Lesley, S.A.
    Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations (2009), Protein Sci., 18, 1081-1094.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the extracellular portion of the membrane associated serine protease solved to high resolution in complex with a nonselective d-FFR chloromethyl ketone inhibitor, in an apo form, in a form where the apo crystal is soaked with the covalent inhibitor camostat and in complex with the protein inhibitor aprotinin. It is also crystallized in the presence of the divalent cation Ca2+ Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens critical role in the regulation of extracellular sodium ion transport via its activation of the epithelial cell sodium channel ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16651
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information critical role in the regulation of extracellular sodium ion transport via its activation of the epithelial cell sodium channel Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
channel-activating protease 1
-
Homo sapiens