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Literature summary for 2.7.10.2 extracted from

  • Nagar, B.; Hantschel, O.; Seeliger, M.; Davies, J.M.; Weis, W.I.; Superti-Furga, G.; Kuriyan, J.
    Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase (2006), Mol. Cell, 21, 787-798.
    View publication on PubMed
Search for more literature for 2.7.10.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged residues 1-531 of splicing variant c-Abl 1b D382N mutant in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged residues 1-531 of splicing variant c-Abl 1b D382N mutant, hanging drop vapor diffusion method, 0.6 ml protein solution mixed with 0.6 ml reservoir solution, in 20% PEG 10000 and 0.1 M HEPES buffer, pH 7.5, at 20ºC, X-ray diffraction structure determination and analysis at 2.27 A resolution, small-angle X-ray scattering data collection and analysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
D382N site-directed mutagenesis, catalytically inactive mutant Homo sapiens
additional information a mutated form of c-Abl, in which the N-terminal cap and two other key contacts in the autoinhibited state are deleted, exists in an extended array of the SH3, SH2, and kinase domains. This alternative conformation of Abl is likely to prolong the active state of the kinase by preventing it from returning to the autoinhibited state, overview Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information c-Abl is inactivated by interactions made by its SH3 and SH2 domains with the distal surface of the kinase domain, a critical N-terminal cap segment, phosphorylated on a serine residue that interacts with the connector between the SH3 and SH2 domains, buttresses the SH3-SH2 substructure in the autoinhibited state and locks it onto the distal surface of the kinase domain, overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens c-Abl is regulated by conformational changes through intramolecular interactions and phosphorylation, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 c-Abl, two splice variants, one c-Abl 1b that is N-terminally myristoylated, and another that is 19 residues shorter at the N-terminus and not known to be myristoylated
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein c-Abl performs autophosphorylation, the N-terminal cap structure is phosphorylated at Ser69, phosphate binding site structure without positively charged residues Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information c-Abl is regulated by conformational changes through intramolecular interactions and phosphorylation, overview Homo sapiens ?
-
 ?
additional information c-Abl performs autophosphorylation Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More enzyme structure analysis, molecular dynamics simulations, structure of the N-terminal cap, residues 65-82, overview Homo sapiens

Synonyms

Synonyms Comment Organism
c-Abl tyrosine kinase
-
 Homo sapiens
nonreceptor tyrosine kinase
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens