|Entry||Database: PDB / ID: 1fpu|
|Title||CRYSTAL STRUCTURE OF ABL KINASE DOMAIN IN COMPLEX WITH A SMALL MOLECULE INHIBITOR|
|Components||PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL|
|Keywords||TRANSFERASE / kinase / kinase inhibitor / STI-571 / activation loop|
|Function / homology|
Function and homology information
Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Cyclin D associated events in G1 / HDR through Single Strand Annealing (SSA) / Myogenesis / RHO GTPases Activate WASPs and WAVEs / Role of ABL in ROBO-SLIT signaling / Regulation of actin dynamics for phagocytic cup formation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / delta-catenin binding / transitional one stage B cell differentiation ...Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Cyclin D associated events in G1 / HDR through Single Strand Annealing (SSA) / Myogenesis / RHO GTPases Activate WASPs and WAVEs / Role of ABL in ROBO-SLIT signaling / Regulation of actin dynamics for phagocytic cup formation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / delta-catenin binding / transitional one stage B cell differentiation / positive regulation of actin filament binding / activation of protein kinase C activity / DNA conformation change / negative regulation of phospholipase C activity / actin filament branching / positive regulation of interleukin-2 secretion / positive regulation blood vessel branching / B cell proliferation involved in immune response / positive regulation of microtubule binding / neuroepithelial cell differentiation / regulation of extracellular matrix organization / positive regulation of Wnt signaling pathway, planar cell polarity pathway / microspike assembly / regulation of modification of synaptic structure / cerebellum morphogenesis / collateral sprouting / B-1 B cell homeostasis / cardiovascular system development / positive regulation of oxidoreductase activity / alpha-beta T cell differentiation / activated T cell proliferation / bubble DNA binding / B cell proliferation / neuropilin signaling pathway / neuropilin binding / regulation of T cell differentiation / regulation of Cdc42 protein signal transduction / negative regulation of protein serine/threonine kinase activity / negative regulation of ubiquitin-protein transferase activity / regulation of microtubule polymerization / negative regulation of BMP signaling pathway / mitogen-activated protein kinase binding / sequence-specific double-stranded DNA binding / regulation of cellular senescence / proline-rich region binding / positive regulation of interferon-gamma secretion / syntaxin binding / negative regulation of cell-cell adhesion / regulation of response to DNA damage stimulus / DNA damage induced protein phosphorylation / negative regulation of cellular senescence / platelet-derived growth factor receptor signaling pathway / positive regulation of osteoblast proliferation / cell leading edge / regulation of axon extension / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of cell migration involved in sprouting angiogenesis / negative regulation of long-term synaptic potentiation / neuromuscular process controlling balance / Bergmann glial cell differentiation / positive regulation of focal adhesion assembly / positive regulation of actin cytoskeleton reorganization / negative regulation of mitotic cell cycle / positive regulation of substrate adhesion-dependent cell spreading / four-way junction DNA binding / phagocytosis / negative regulation of endothelial cell apoptotic process / endothelial cell migration / positive regulation of stress fiber assembly / regulation of actin cytoskeleton organization / signal transduction in response to DNA damage / substrate adhesion-dependent cell spreading / positive regulation of endothelial cell migration / spleen development / SH2 domain binding / post-embryonic development / neural tube closure / negative regulation of I-kappaB kinase/NF-kappaB signaling / positive regulation of mitotic cell cycle / ruffle / positive regulation of release of sequestered calcium ion into cytosol / thymus development / protein kinase C binding / negative regulation of ERK1 and ERK2 cascade / phosphotyrosine residue binding / neuron differentiation / ephrin receptor binding / integrin-mediated signaling pathway / actin cytoskeleton organization / autophagy / regulation of cell cycle / non-specific protein-tyrosine kinase / peptidyl-tyrosine autophosphorylation / epidermal growth factor receptor signaling pathway / non-membrane spanning protein tyrosine kinase activity / establishment of protein localization / actin cytoskeleton / SH3 domain binding / cellular response to hydrogen peroxide / positive regulation of neuron death
SH2 domain / Tyrosine-protein kinase ABL, SH2 domain / Protein kinases ATP-binding region signature. / F-actin binding / Protein kinase domain / SH3 domain / SH2 domain / SH2 domain superfamily / SH3-like domain superfamily / Tyrosine-protein kinase ABL1/transforming protein Abl ...SH2 domain / Tyrosine-protein kinase ABL, SH2 domain / Protein kinases ATP-binding region signature. / F-actin binding / Protein kinase domain / SH3 domain / SH2 domain / SH2 domain superfamily / SH3-like domain superfamily / Tyrosine-protein kinase ABL1/transforming protein Abl / Src homology 2 (SH2) domain profile. / Tyrosine-protein kinase, catalytic domain / Protein kinase, ATP binding site / F-actin binding / Protein kinase-like domain superfamily / Tyrosine-protein kinase, active site / SH3 domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Protein tyrosine kinase / Src homology 3 (SH3) domain profile. / Protein kinase domain profile.
Tyrosine-protein kinase ABL1
|Biological species||Mus musculus (house mouse)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.4 Å|
|Authors||Schindler, T. / Bornmann, W. / Pellicena, P. / Miller, W.T. / Clarkson, B. / Kuriyan, J.|
|Citation||Journal: Science / Year: 2000|
Title: Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.
Authors: Schindler, T. / Bornmann, W. / Pellicena, P. / Miller, W.T. / Clarkson, B. / Kuriyan, J.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
B: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
A: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
B: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL
|Details||There are two kinase molecules in the asymmetric unit. The biological assembly is a monomer.|
Mass: 33743.523 Da / Num. of mol.: 2 / Fragment: KINASE DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PFASTBAC / Cell line (production host): SF9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P00520, EC: 126.96.36.199
Mass: 382.418 Da / Num. of mol.: 2 / Fragment: 2-(PHENYLAMINO)-PYRIMIDINE COMPOUND / Source method: obtained synthetically / Formula: C22H18N6O
Details: chemically synthesized as described in Zimmermann J., Buchdunger E., Mett H., Meyer T., Lydon N.B. (1997) Bioorg. Med. Chem. Lett., Vol. 7, pp. 187
|#3: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.29 Å3/Da / Density % sol: 46.24 %|
|Crystal grow||Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.2 |
Details: PEG 4000, magnesium chloride, mes, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K
*PLUSTemperature: 4 ℃ / pH: 8
|Components of the solutions|
|Diffraction||Mean temperature: 103 K|
|Diffraction source||Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 0.9393|
|Detector||Type: BRANDEIS - B4 / Detector: CCD / Date: Sep 5, 1999|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 0.9393 Å / Relative weight: 1|
|Reflection||Resolution: 2.4→99 Å / Num. obs: 221636 / % possible obs: 98.7 % / Redundancy: 9.3 % / Biso Wilson estimate: 61 Å2 / Rmerge(I) obs: 0.068 / Net I/σ(I): 30.9|
|Reflection shell||Resolution: 2.4→2.49 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.216 / Num. unique all: 2190 / % possible all: 90.6|
*PLUSNum. obs: 24122 / Num. measured all: 221636
*PLUS% possible obs: 90.6 %
|Refinement||Resolution: 2.4→99 Å / Stereochemistry target values: Engh & Huber|
Details: Tight, noncrystallographic restraints were utilized throughout the refinement so that the final r.m.s. deviation between the two molecules is 0.05 and 0.04 Angstrom for the N-terminal and the C-terminal lobes, respectively (excluding residues 229 to 337, 252, 262, 271, 294, 306, 404, 447, 450, 466, and 491, which were built in different conformations in the two molecules). The electron density map was significantly weaker for one of the two molecules in the asymmetric unit (chain ID B), and all the analysis (cf. primary citation) relied on the better-ordered one (chain ID A).
|Refinement step||Cycle: LAST / Resolution: 2.4→99 Å|
|Refine LS restraints|
*PLUSName: CNS / Classification: refinement
*PLUSHighest resolution: 2.4 Å / Lowest resolution: 99 Å / Rfactor obs: 0.239
|Refine LS restraints|
*PLUSType: c_angle_deg / Dev ideal: 1.4
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