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- PDB-1tce: SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYR... -
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Basic information
Entry | Database: PDB / ID: 1tce | ||||||
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Title | SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE | ||||||
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![]() | COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) / SH2 DOMAIN / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) complex | ||||||
Function / homology | ![]() regulation of superoxide metabolic process / gamma-delta T cell receptor complex / positive regulation of cell proliferation in bone marrow / Fc-gamma receptor III complex / Fc-gamma receptor signaling pathway / gamma-delta T cell activation / XBP1(S) activates chaperone genes / neurotrophin TRKA receptor binding / alpha-beta T cell receptor complex / positive regulation of protein localization to cell surface ...regulation of superoxide metabolic process / gamma-delta T cell receptor complex / positive regulation of cell proliferation in bone marrow / Fc-gamma receptor III complex / Fc-gamma receptor signaling pathway / gamma-delta T cell activation / XBP1(S) activates chaperone genes / neurotrophin TRKA receptor binding / alpha-beta T cell receptor complex / positive regulation of protein localization to cell surface / transmembrane receptor protein tyrosine kinase adaptor activity / Nef and signal transduction / Interleukin-15 signaling / Interleukin-2 signaling / Shc-EGFR complex / epidermal growth factor binding / T cell receptor complex / epidermal growth factor receptor binding / Signaling by ALK / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / alpha-beta T cell activation / Generation of second messenger molecules / RET signaling / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / FCGR activation / Interleukin-3, Interleukin-5 and GM-CSF signaling / SHC1 events in ERBB4 signaling / PD-1 signaling / Signalling to RAS / Role of phospholipids in phagocytosis / SHC-related events triggered by IGF1R / Role of LAT2/NTAL/LAB on calcium mobilization / Signal attenuation / Interleukin receptor SHC signaling / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / SHC-mediated cascade:FGFR1 / Erythropoietin activates RAS / Signaling by CSF3 (G-CSF) / Tie2 Signaling / SHC1 events in EGFR signaling / ephrin receptor binding / phosphotyrosine residue binding / SHC1 events in ERBB2 signaling / Integrin signaling / Constitutive Signaling by Overexpressed ERBB2 / FCERI mediated Ca+2 mobilization / Insulin receptor signalling cascade / negative regulation of angiogenesis / FCGR3A-mediated IL10 synthesis / protein tyrosine kinase binding / insulin-like growth factor receptor signaling pathway / FCERI mediated MAPK activation / FCGR3A-mediated phagocytosis / Signaling by ERBB2 TMD/JMD mutants / insulin-like growth factor receptor binding / Constitutive Signaling by EGFRvIII / insulin receptor binding / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / epidermal growth factor receptor signaling pathway / phospholipid binding / receptor tyrosine kinase binding / Regulation of actin dynamics for phagocytic cup formation / cellular response to growth factor stimulus / cell-cell adhesion / transmembrane signaling receptor activity / GPER1 signaling / Signaling by CSF1 (M-CSF) in myeloid cells / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Signaling by ALK fusions and activated point mutants / Downstream TCR signaling / insulin receptor signaling pathway / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / DAP12 signaling / protein complex oligomerization / heart development / T cell receptor signaling pathway / actin cytoskeleton organization / RAF/MAP kinase cascade / protein-containing complex assembly / angiogenesis / adaptive immune response / positive regulation of MAPK cascade / Extra-nuclear estrogen signaling / cell surface receptor signaling pathway / positive regulation of ERK1 and ERK2 cascade / intracellular signal transduction / mitochondrial matrix / defense response to bacterium / protein heterodimerization activity / focal adhesion / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / negative regulation of apoptotic process / positive regulation of DNA-templated transcription Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Zhou, M.-M. / Meadows, R.P. / Logan, T.M. / Yoon, H.S. / Wade, W.R. / Ravichandran, K.S. / Burakoff, S.J. / Feisk, S.W. | ||||||
![]() | ![]() Title: Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Authors: Zhou, M.M. / Meadows, R.P. / Logan, T.M. / Yoon, H.S. / Wade, W.S. / Ravichandran, K.S. / Burakoff, S.J. / Fesik, S.W. #1: ![]() Title: Nuclear Magnetic Resonance Structure of an Sh2 Domain of Phospholipase C-Gamma 1 Complexed with a High Affinity Binding Peptide Authors: Pascal, S.M. / Singer, A.U. / Gish, G. / Yamazaki, T. / Shoelson, S.E. / Pawson, T. / Kay, L.E. / Forman-Kay, J.D. #2: ![]() Title: Binding of a High Affinity Phosphotyrosyl Peptide to the Src Sh2 Domain: Crystal Structures of the Complexed and Peptide-Free Forms Authors: Waksman, G. / Shoelson, S.E. / Pant, N. / Cowburn, D. / Kuriyan, J. #3: ![]() Title: Recognition of a High-Affinity Phosphotyrosyl Peptide by the Src Homology-2 Domain of P56Lck Authors: Eck, M.J. / Shoelson, S.E. / Harrison, S.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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-Validation report
Summary document | ![]() | 259.6 KB | Display | ![]() |
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Full document | ![]() | 259.4 KB | Display | |
Data in XML | ![]() | 4.8 KB | Display | |
Data in CIF | ![]() | 6.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 12123.677 Da / Num. of mol.: 1 / Fragment: SH2 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1529.545 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P20963 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||
Refinement | Software ordinal: 1 Details: SET OF IDEAL BOND LENGTHS AND ANGLES USED DURING REFINEMENT: PARALLHDG.PRO IN X-PLOR. | ||||||||
NMR ensemble | Conformers submitted total number: 1 |