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3.4.21.73: u-Plasminogen activator

This is an abbreviated version!
For detailed information about u-Plasminogen activator, go to the full flat file.

Word Map on EC 3.4.21.73

Reaction

Specific cleavage of Arg-/-Val bond in plasminogen to form plasmin =

Synonyms

Abbokinase, Cellular plasminogen activator, Double-chain urokinase-type plasminogen activator, EC 3.4.21.31, EC 3.4.99.26, Plasminogen activator, urokinase-type, PLAU, Two-chain urokinase-type plasminogen activator, u-PA, U-plasminogen activator, UK, uPA, uPA-type Plg activator, Urinary esterase A, Urinary plasminogen activator, Urokinase, Urokinase plasminogen activator, urokinase type plasminogen activator, urokinase-plasminogen activator, urokinase-type PA, urokinase-type plasmin activator, urokinase-type plasminogen, Urokinase-type plasminogen activator, urokinase-type Plg activator, urokine-type plasminogen activator

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.73 u-Plasminogen activator

Crystallization

Crystallization on EC 3.4.21.73 - u-Plasminogen activator

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-c-uPA in complex with inhibitor UPA-I1, space group P2(1)2(1)2(1), cell constants a = 53.2 A, b = 54.7 A, c = 82.4 A, beta-c-uPA in complex with inhibitor UPA-I3, space group P2(1)2(1)2(1), cell constants a = 52.9 A, b = 54.7 A, c = 81.4 A, beta-c-uPA in complex with inhibitor UPA-I2, space group P2(1)2(1)2(1), cell constants a = 53.0 A, b = 54.4 A, c = 82.2 A, beta-c-uPA in complex with inhibitor UPA-I5, space group P2(1)2(1)2(1), cell constants a = 53.0 A, b = 54.9 A, c = 82.3 A, beta-c-uPA in complex with inhibitor UPA-I6, space group P2(1)2(1)2(1), cell constants a = 53.5 A, b = 54.8 A, c = 82.4 A, complex by soaking, Ybeta-c-uPA in complex with inhibitor UPA-I6, space group P4(3)2(1)2, cell constants a = 76.7 A, b = 76.7 A, c = 127.5 A, complex by Co-crystallization, beta-c-uPA in complex with inhibitor UPA-I4, space group P4(1)2(1)2, cell constants a = 55.0 A, b = 55.0 A, c = 151.6 A, complex by Co-crystallization
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crystal structure of the catalytic domain of the recombinant nonglycosylated human uPA, complexed with the inhibitor Glu-Gly-Arg chloromethyl ketone at 2.5 A
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crystallized by vapor diffusion in hanging drops in complex with 4-iodobenzo[b]thiophene-2-carboxamidine and benzamidine, space group C2, ProteinDataBank accession code 1C5Z for uPA-benzamidine, 1C5Y for uPA-thieno[2,3-b]pyridine-2-carboxamidine
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in complex with inhibitor N-[(4-chlorobenzyl)sulfonyl]-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide, N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-serinamide and N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)glycinamide
N-terminal fragment, in complex with urokinase receptor and an antibody against the receptor
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PAI-1/uPA mutant S195A in a Michaelis complex, hanging drop method, 20°C, mixing of equal volumes of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 150 mM NaCl, and precipitant solution, containing 1.4 M ammonium sulfate and 0.1 M Tris-HCl, pH 7.4, 4 months, the cryoprotectant solution contains 30% glycerol, 1.6 M ammonium sulfate, and 0.1 M Tris-HCl, pH 7.4, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
purified amino-terminal fragment of urokinase-type plasminogen activator, free and complexed with uPA receptor, lacking the cell-surface anchoring sequence, hanging-drop vapor-diffusion method, room temperature, 0.003 ml of 20 or 8 mg/ml protein, respectively, in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, is mixed with an equal volume of reservoir solution containing 100 mM Ches, pH 10.5, 1.2 M sodium dihydrogen phosphate, 0.8 M potassium hydrogen phosphate, 200 mM lithium sulfate for the free enzyme or 100 mM Bis-Tris, pH 5.5, 22.5% w/v PEG 3350, 200 mM ammonium sulfate for the enzyme fragment-receptor complex, 1 week, cryoprotection by 15% v/v glycerol, X-ray diffraction structure determination and anaylsis at 1.9-3.3 A resolution, molecular modeling
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purified recombinant enzyme mutant H99Y in complex with mupain-1 inhibitor variants, sitting drop vapour diffusion method, equilibrating of protein against a reservoir solution containing 2.0 M ammonium sulfate, 50 mM sodium citrate, pH 4.6, and 5% PEG 400, room temperature, about 3 days, soaking of crystals in 40% PEG 4000, 100 mM Tris-HCl, pH 7.4 containing 1 mM mupain ligand variant, X-ray diffraction structure determination and analysis at 1.6 A resolution
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recombinant amino-terminal fragment S1-E143 expressed in Pichia pastoris
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solution structure of the kringle domain
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in complex with inhibitors mexiletine and 4-(2-aminoethoxy)-N-(3-chloro-2-ethoxy-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamide
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