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Literature summary for 3.4.24.87 extracted from

  • Zanardelli, S.; Chion, A.C.; Groot, E.; Lenting, P.J.; McKinnon, T.A.; Laffan, M.A.; Tseng, M.; Lane, D.A.
    A novel binding site for ADAMTS13 constitutively exposed on the surface of globular VWF (2009), Blood, 114, 2819-2828.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.87

Protein Variants

Protein Variants Comment Organism
additional information construction of ADAMTS13 truncated mutants, MDTCS and del(TSP5-CUB), and analysis of their binding with different C-terminal domain VWF fragments, overview Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information C-terminal VWF fragments, as well as an antibody specifically directed toward the VWF D4 domain, inhibit VWF proteolysis by ADAMTS13 under shear conditions Homo sapiens
VWFA2 domain a C-terminal 32 kDa fragment of VWF, soluble VWFA2 domain effectively inhibits the binding of ADAMTS13 to immobilized VWFA2, and completely inhibits the interaction between ADAMTS13 and immobilized 64 kDa VWFA1A2A3 fragment Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens proteolysis can occur only once VWF has been unraveled from its globular conformation, either by high fluid shear stress in vivo or in the presence of denaturants in vitro, conditions that are able to promote the exposure of the VWF scissile bond ?
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 ?
von Willebrand factor + H2O Homo sapiens ADAMTS-13 cleaves the Tyr1605-Met1606 bond in the VWF A2 domain, mechanisms of VWF recognition, cleavage analysis and kinetics under static and flow conditions, overview von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information proteolysis can occur only once VWF has been unraveled from its globular conformation, either by high fluid shear stress in vivo or in the presence of denaturants in vitro, conditions that are able to promote the exposure of the VWF scissile bond Homo sapiens ?
-
 ?
additional information proteolysis can occur only once VWF has been unraveled from its globular conformation, either by high fluid shear stress in vivo or in the presence of denaturants in vitro, conditions that are able to promote the exposure of the VWF scissile bond. The ADAMTS13 C-terminal distal domains (TSP5-CUB) bind to a novel binding site in the C-terminal region of VWF, spanning residues 1874-2813 and including the VWF D4 domain, which, critically, is constitutively exposed on the surface of VWF in solution without flow. C-terminal VWF fragments, as well as an antibody specifically directed toward the VWF D4 domain, inhibit VWF proteolysis by ADAMTS13 under shear conditions Homo sapiens ?
-
 ?
von Willebrand factor + H2O ADAMTS-13 cleaves the Tyr1605-Met1606 bond in the VWF A2 domain, mechanisms of VWF recognition, cleavage analysis and kinetics under static and flow conditions, overview Homo sapiens von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
-
 ?
von Willebrand factor + H2O ADAMTS-13 cleaves the Tyr1605-Met1606 bond in the VWF A2 domain, mechanisms of VWF recognition. One ADAMTS13 binding site of VWF is located in the region of VWF spanning residues 1874 to 2813, which includes the VWF D4 domain, interacts with the C-terminal domains of ADAMTS13, interaction occurs even when VWF is in static conditions, globular and with the VWF A2 domain hidden. The binding site may participate as the initial step of a multistep interaction ultimately leading to proteolysis of VWF byADAMTS13 Homo sapiens von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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 ?

Synonyms

Synonyms Comment Organism
ADAMTS13
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 Homo sapiens
ADAMTS13 metalloprotease
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information C-terminal fragments competitive inhibition binding, kinetics, overview Homo sapiens
0.000028
-
 VWFA2 domain pH 7.8, 37°C Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.000072
-
 pH 7.8, 37°C Homo sapiens VWFA2 domain

General Information

General Information Comment Organism
physiological function ADAMTS13 metalloprotease regulates the multimeric size of von Willebrand factor Homo sapiens