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Yorodumi- PDB-1awo: THE SOLUTION NMR STRUCTURE OF ABL SH3 AND ITS RELATIONSHIP TO SH2... -
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-Basic information
Entry | Database: PDB / ID: 1awo | ||||||
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Title | THE SOLUTION NMR STRUCTURE OF ABL SH3 AND ITS RELATIONSHIP TO SH2 IN THE SH(32) CONSTRUCT, 20 STRUCTURES | ||||||
Components | ABL TYROSINE KINASE | ||||||
Keywords | KINASE / SH3 DOMAIN / TRANSFERASE / PHOSPHOTRANSFERASE / PROTO-ONCOGENE / MULTIPLE DOMAIN / LEUKEMIA | ||||||
Function / homology | Function and homology information negative regulation of phospholipase C activity / positive regulation of actin filament binding / positive regulation of oxidoreductase activity / transitional one stage B cell differentiation / protein localization to cytoplasmic microtubule plus-end / DNA conformation change / podocyte apoptotic process / DN4 thymocyte differentiation / Role of ABL in ROBO-SLIT signaling / response to epinephrine ...negative regulation of phospholipase C activity / positive regulation of actin filament binding / positive regulation of oxidoreductase activity / transitional one stage B cell differentiation / protein localization to cytoplasmic microtubule plus-end / DNA conformation change / podocyte apoptotic process / DN4 thymocyte differentiation / Role of ABL in ROBO-SLIT signaling / response to epinephrine / activation of protein kinase C activity / nicotinate-nucleotide adenylyltransferase activity / regulation of modification of synaptic structure / positive regulation of extracellular matrix organization / positive regulation of microtubule binding / delta-catenin binding / B cell proliferation involved in immune response / neuroepithelial cell differentiation / microspike assembly / positive regulation of Wnt signaling pathway, planar cell polarity pathway / cerebellum morphogenesis / positive regulation of blood vessel branching / B-1 B cell homeostasis / mitochondrial depolarization / negative regulation of ubiquitin-protein transferase activity / neuropilin signaling pathway / neuropilin binding / bubble DNA binding / regulation of Cdc42 protein signal transduction / negative regulation of protein serine/threonine kinase activity / activated T cell proliferation / cellular response to dopamine / regulation of cell motility / regulation of axon extension / proline-rich region binding / positive regulation of dendrite development / mitogen-activated protein kinase binding / myoblast proliferation / alpha-beta T cell differentiation / regulation of hematopoietic stem cell differentiation / syntaxin binding / cardiac muscle cell proliferation / HDR through Single Strand Annealing (SSA) / regulation of T cell differentiation / negative regulation of double-strand break repair via homologous recombination / positive regulation of cell migration involved in sprouting angiogenesis / Fc-gamma receptor signaling pathway involved in phagocytosis / negative regulation of cell-cell adhesion / Myogenesis / regulation of microtubule polymerization / positive regulation of osteoblast proliferation / RUNX2 regulates osteoblast differentiation / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of focal adhesion assembly / negative regulation of cellular senescence / negative regulation of long-term synaptic potentiation / Bergmann glial cell differentiation / associative learning / neuromuscular process controlling balance / regulation of endocytosis / actin monomer binding / negative regulation of BMP signaling pathway / negative regulation of mitotic cell cycle / mismatch repair / endothelial cell migration / RHO GTPases Activate WASPs and WAVEs / positive regulation of T cell migration / canonical NF-kappaB signal transduction / BMP signaling pathway / negative regulation of endothelial cell apoptotic process / regulation of cell adhesion / positive regulation of substrate adhesion-dependent cell spreading / four-way junction DNA binding / signal transduction in response to DNA damage / peptidyl-tyrosine autophosphorylation / positive regulation of vasoconstriction / spleen development / positive regulation of stress fiber assembly / ruffle / ERK1 and ERK2 cascade / cellular response to transforming growth factor beta stimulus / positive regulation of establishment of T cell polarity / positive regulation of interleukin-2 production / actin filament polymerization / SH2 domain binding / response to endoplasmic reticulum stress / phosphotyrosine residue binding / ephrin receptor binding / positive regulation of mitotic cell cycle / substrate adhesion-dependent cell spreading / post-embryonic development / protein kinase C binding / positive regulation of release of sequestered calcium ion into cytosol / positive regulation of endothelial cell migration / thymus development / regulation of autophagy / neural tube closure / integrin-mediated signaling pathway / establishment of localization in cell / regulation of actin cytoskeleton organization Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / VARIABLE TARGET FUNCTION TORSION ANGLE SIMULATED ANNEALING | ||||||
Authors | Cowburn, D. | ||||||
Citation | Journal: Structure / Year: 1995 Title: The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct. Authors: Gosser, Y.Q. / Zheng, J. / Overduin, M. / Mayer, B.J. / Cowburn, D. #1: Journal: Mol.Cell.Biol. / Year: 1994 Title: Mutagenic Analysis of the Roles of Sh2 and SH3 Domains in Regulation of the Abl Tyrosine Kinase Authors: Mayer, B.J. / Baltimore, D. #2: Journal: Nat.Struct.Biol. / Year: 1994 Title: High-Resolution Crystal Structures of Tyrosine Kinase SH3 Domains Complexed with Proline-Rich Peptides Authors: Musacchio, A. / Saraste, M. / Wilmanns, M. #3: Journal: Science / Year: 1993 Title: Identification of a Ten-Amino Acid Proline-Rich SH3 Binding Site Authors: Ren, R. / Mayer, B.J. / Cicchetti, P. / Baltimore, D. #4: Journal: Embo J. / Year: 1993 Title: Crystal Structure of the SH3 Domain in Human Fyn; Comparison of the Three-Dimensional Structures of SH3 Domains in Tyrosine Kinases and Spectrin Authors: Noble, M.E. / Musacchio, A. / Saraste, M. / Courtneidge, S.A. / Wierenga, R.K. #5: Journal: Cell(Cambridge,Mass.) / Year: 1992 Title: Three-Dimensional Solution Structure of the Src Homology 2 Domain of C-Abl Authors: Overduin, M. / Rios, C.B. / Mayer, B.J. / Baltimore, D. / Cowburn, D. #6: Journal: Nature / Year: 1992 Title: Crystal Structure of a Src-Homology 3 (SH3) Domain Authors: Musacchio, A. / Noble, M. / Pauptit, R. / Wierenga, R. / Saraste, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1awo.cif.gz | 337.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1awo.ent.gz | 291.4 KB | Display | PDB format |
PDBx/mmJSON format | 1awo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aw/1awo ftp://data.pdbj.org/pub/pdb/validation_reports/aw/1awo | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6637.299 Da / Num. of mol.: 1 / Fragment: SRC-HOMOLOGY 3 (SH3) DOMAIN / Mutation: N64S, N120S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: EXPRESSED AS GST FUSIONS AND CLEAVED / Plasmid: PGEX / Production host: Escherichia coli (E. coli) / Strain (production host): NB42 / References: UniProt: P00519, EC: 2.7.1.112 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 7.5 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: VARIABLE TARGET FUNCTION TORSION ANGLE SIMULATED ANNEALING Software ordinal: 1 / Details: USED REDAC STRATEGY | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST TARGET FUNCTION / Conformers calculated total number: 100 / Conformers submitted total number: 20 |