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3.4.21.76: Myeloblastin

This is an abbreviated version!
For detailed information about Myeloblastin, go to the full flat file.

Word Map on EC 3.4.21.76

Reaction

Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-/- > -Val-/- =

Synonyms

AGP7, C-ANCA antigen, hPR-3, human leukocyte proteinase 3, human PR3, human proteinase 3, Leukocyte proteinase 3, Leukocyte proteinase 4, membrane proteinase 3, membrane-associated proteinase 3, mP3, mPR3, myeloblastin, neutrophil protease PR3, neutrophil proteinase 3, neutrophil serine protease, neutrophilic serine protease proteinase 3, P29, p29b, PMNL proteinase, Pr 3, PR-3, PR3, protease 3, proteinase 3, Proteinase PR-3, Proteinase-3, proteinase3, PRTN3, SAP3, secreted aspartic proteinase 3, surface proteinase 3, Wegener autoantigen, Wegener's autoantigen, Wegener's granulomatosis autoantigen, Xenopus PR3, xPR-3

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.76 Myeloblastin

Crystallization

Crystallization on EC 3.4.21.76 - Myeloblastin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sap3 in a stable complex with pepstatin A and in the absence of an inhibitor, in the presence of Zn2+, to 1.9 and 2.2 A resolution. Inhibitor binding causes active site closure by the movement of a flap segment. Sap3 consists of the S2' binding site becoming channelshaped subsequent to the turn of the loop with residues 129–135
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adopts a fold consisting of two beta-barrels made each of six anti-parallel beta-sheets. Crystallizes as a tetramer, which can be regarded as a dimer of dimers: two monomers in a dimer are oriented so that their active sites face each other, preventing the binding of large substrates. The hole in the middle of the tetramer is lined with hydrophobic residues. Contains four disulfide bridges between cysteine pairs 42-58, 136-201, 168-182 and 191-220. No X-ray structure of PR3 with a substrate in its active site available
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crystal structure of recombinant PR3. Overall fold consists of two beta-barrel domains. PR3 structure includes a disaccharide unit covalently attached to Asn159. PR3 substrate binding sites at S4 to S3'
molecular dynamics simulations of PR3 anchored at three different phospholipid bilayers: dimyristoylphosphatidylcholine DMPC and dimyristoylphosphatidylglycerol DMPG, and an equimolar mixture of DMPC/DMPG. Basic residues R177, R186A, R186B, K187 and R222 interact via hydrogen bonds with the lipid headgroups to stabilize PR3 at the interfacial membrane region. Hydrophobic amino acids V163, F165, F166, I217, L223, and F224 insert into the hydrophobic core below the carbonyl groups of the bilayers and aromatic amino acids F165, F192, F215, W218, F224, and F227 contribute electrostatic interaction via cation-pi interactions with the choline groups of DMPC. PR3 presents all the characteristics of a peripheral membrane protein with an ability to bind negative phospholipids. The catalytic triad remains unperturbed by the presence of the membrane, the ligand binding sites are located in close proximity to the membrane and amino acids K99 and I217 interact significantly with the lipids
to 2.2 A resolution
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