+Open data
-Basic information
Entry | Database: PDB / ID: 1hct | ||||||
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Title | NMR STRUCTURE OF THE HUMAN SRC SH2 DOMAIN COMPLEX | ||||||
Components |
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Keywords | COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) / HUMAN PP60C-SRC SH2 DOMAIN / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) COMPLEX | ||||||
Function / homology | Function and homology information regulation of toll-like receptor 3 signaling pathway / positive regulation of non-membrane spanning protein tyrosine kinase activity / primary ovarian follicle growth / regulation of caveolin-mediated endocytosis / positive regulation of ovarian follicle development / cellular response to prolactin / positive regulation of platelet-derived growth factor receptor-beta signaling pathway / positive regulation of male germ cell proliferation / dendritic filopodium / regulation of cell projection assembly ...regulation of toll-like receptor 3 signaling pathway / positive regulation of non-membrane spanning protein tyrosine kinase activity / primary ovarian follicle growth / regulation of caveolin-mediated endocytosis / positive regulation of ovarian follicle development / cellular response to prolactin / positive regulation of platelet-derived growth factor receptor-beta signaling pathway / positive regulation of male germ cell proliferation / dendritic filopodium / regulation of cell projection assembly / regulation of cell-cell adhesion / response to mineralocorticoid / positive regulation of dephosphorylation / Regulation of commissural axon pathfinding by SLIT and ROBO / ERBB2 signaling pathway / regulation of epithelial cell migration / entry of bacterium into host cell / positive regulation of protein transport / Regulation of gap junction activity / BMP receptor binding / positive regulation of lamellipodium morphogenesis / cellular response to progesterone stimulus / regulation of vascular permeability / Activated NTRK2 signals through FYN / positive regulation of integrin activation / negative regulation of focal adhesion assembly / positive regulation of protein processing / skeletal muscle cell proliferation / : / intestinal epithelial cell development / Netrin mediated repulsion signals / regulation of intracellular estrogen receptor signaling pathway / CD28 co-stimulation / positive regulation of glucose metabolic process / transcytosis / osteoclast development / Activated NTRK3 signals through PI3K / connexin binding / cellular response to fluid shear stress / response to acidic pH / focal adhesion assembly / signal complex assembly / positive regulation of small GTPase mediated signal transduction / positive regulation of Ras protein signal transduction / podosome / regulation of bone resorption / positive regulation of podosome assembly / Regulation of RUNX1 Expression and Activity / branching involved in mammary gland duct morphogenesis / adherens junction organization / DCC mediated attractive signaling / myoblast proliferation / EPH-Ephrin signaling / odontogenesis / negative regulation of mitochondrial depolarization / Ephrin signaling / cellular response to peptide hormone stimulus / Signal regulatory protein family interactions / cellular response to fatty acid / MET activates PTK2 signaling / regulation of early endosome to late endosome transport / Regulation of KIT signaling / Signaling by ALK / postsynaptic specialization, intracellular component / Receptor Mediated Mitophagy / GP1b-IX-V activation signalling / CTLA4 inhibitory signaling / oogenesis / phospholipase activator activity / leukocyte migration / interleukin-6-mediated signaling pathway / DNA biosynthetic process / Fc-gamma receptor signaling pathway involved in phagocytosis / EPHA-mediated growth cone collapse / p130Cas linkage to MAPK signaling for integrins / positive regulation of Notch signaling pathway / cellular response to platelet-derived growth factor stimulus / Signaling by EGFR / stress fiber assembly / positive regulation of epithelial cell migration / positive regulation of smooth muscle cell migration / negative regulation of hippo signaling / progesterone receptor signaling pathway / regulation of heart rate by cardiac conduction / RUNX2 regulates osteoblast differentiation / dendritic growth cone / Recycling pathway of L1 / stimulatory C-type lectin receptor signaling pathway / PECAM1 interactions / uterus development / phospholipase binding / GRB2:SOS provides linkage to MAPK signaling for Integrins / Long-term potentiation / neurotrophin TRK receptor signaling pathway / negative regulation of telomere maintenance via telomerase / RHOU GTPase cycle / platelet-derived growth factor receptor signaling pathway / negative regulation of anoikis / RET signaling / FCGR activation Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Gampe Junior, R.T. / Xu, R.X. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide. Authors: Xu, R.X. / Word, J.M. / Davis, D.G. / Rink, M.J. / Willard Jr., D.H. / Gampe Jr., R.T. #1: Journal: J.Biol.Chem. / Year: 1994 Title: Peptide Inhibitors of Src SH3-Sh2(Slash)Phosphoprotein Interactions Authors: Gilmer, T. / Rodriguez, M. / Jordan, S. / Crosby, R. / Alligood, K. / Green, M. / Kimery, M. / Wagner, C. / Kinder, D. / Charifson, P. / Hassell, A.M. / Willard, D. / Luther, M. / Rusnak, D. ...Authors: Gilmer, T. / Rodriguez, M. / Jordan, S. / Crosby, R. / Alligood, K. / Green, M. / Kimery, M. / Wagner, C. / Kinder, D. / Charifson, P. / Hassell, A.M. / Willard, D. / Luther, M. / Rusnak, D. / Sternbach, D.D. / Mehrotra, M. / Peel, M. / Shampine, L. / Davis, R. / Robbins, J. / Patel, I.R. / Kassel, D. / Burkhart, W. / Moyer, M. / Bradshaw, T. / Berman, J. #2: Journal: Cell(Cambridge,Mass.) / Year: 1994 Title: Nuclear Magnetic Resonance Structure of an Sh2 Domain of Phospholipase C-Gamma1 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. #3: Journal: Cell(Cambridge,Mass.) / Year: 1993 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. #4: Journal: Nature / Year: 1993 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. #5: Journal: Mol.Cell.Biol. / Year: 1985 Title: Human Cellular Src Gene: Nucleotide Sequence and Derived Amino Acid Sequence of the Region Coding for the Carboxy-Terminal Two-Thirds of Pp60C-Src Authors: Anderson, S.K. / Gibbs, C.P. / Tanaka, A. / Kung, H.J. / Fugita, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hct.cif.gz | 874.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hct.ent.gz | 760 KB | Display | PDB format |
PDBx/mmJSON format | 1hct.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hc/1hct ftp://data.pdbj.org/pub/pdb/validation_reports/hc/1hct | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 787.705 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
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#2: Protein | Mass: 12303.886 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NUCLEOTIDE SEQUENCE A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P12931 |
-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: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
NMR ensemble | Conformers submitted total number: 23 |