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Literature summary for 3.1.4.39 extracted from

  • Hausmann, J.; Kamtekar, S.; Christodoulou, E.; Day, J.E.; Wu, T.; Fulkerson, Z.; Albers, H.M.; van Meeteren, L.A.; Houben, A.J.; van Zeijl, L.; Jansen, S.; Andries, M.; Hall, T.; Pegg, L.E.; Benson, T.E.; Kasiem, M.; Harlos, K.; Kooi, C.W.; Smyth, S.S.; Ovaa, H.; Bollen, M.; Morris, A.J.; Moolenaar, W.H.; Perrakis, A.
    Structural basis of substrate discrimination and integrin binding by autotaxin (2011), Nat. Struct. Mol. Biol., 18, 198-204.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.39

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, ATX alone and in complex with a small-molecule inhibitor HA155, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement and single-wavelength anomalous dispersion Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
A218V site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus
A305E site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus
F211A site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus
F274E site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus
F275Q site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus
L214H site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus
S170E site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus
Y307Q site-directed mutagenesis, a hydrophobic binding pocket mutant, the mutant shows reduced lysoPLD activity levels compared to the wild-type Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
HA155 the boron atom on one end of the inhibitor forms a reversible covalent bond with the nucleophile hydroxyl group of Thr209. One of the two boron hydroxyl groups is further stabilized between the two zinc ions, binding structure, overview Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, active site bound Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
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 about Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus binding of ATX to activated platelets and lymphocytes in an integrin-dependent manner mediated by the consecutive cysteine-rich somatomedin-B-like, SMB, domains ?
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus Q64610
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information binding of ATX to activated platelets and lymphocytes in an integrin-dependent manner mediated by the consecutive cysteine-rich somatomedin-B-like, SMB, domains Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
More ATX has several distinct domains. At the N-terminus it harbours two consecutive cysteine-rich somatomedin-B-like, SMB, domains, a fold known to be involved in protein-protein interactions. The central catalytic phosphodiesterase, PDE, domain follows the SMB domains. At its C-terminus, ATX contains a nuclease-like, NUC, domain, which is catalytically inert and might be involved in substrate binding and presentation Rattus norvegicus

Synonyms

Synonyms Comment Organism
ATX
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 Rattus norvegicus
autotaxin
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 Rattus norvegicus

General Information

General Information Comment Organism
additional information structural basis of substrate discrimination and integrin binding by autotaxin, ATX, that interacts with cell-surface integrins via its N-terminal somatomedin-B-like domains, using an atypical mechanism, overview Rattus norvegicus
physiological function ATX promotes localized LPA signaling Rattus norvegicus