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- PDB-1tce: SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYR... -

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Entry
Database: PDB / ID: 1tce
TitleSOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE
Components
  • PHOSPHOPEPTIDE OF THE ZETA CHAIN OF T CELL RECEPTOR
  • SHC
KeywordsCOMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) / SH2 DOMAIN / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) complex
Function / homology
Function and homology information


regulation of superoxide metabolic process / positive regulation of cell proliferation in bone marrow / gamma-delta T cell receptor complex / Fc-gamma receptor III complex / gamma-delta T cell activation / Fc-gamma receptor signaling pathway / XBP1(S) activates chaperone genes / neurotrophin TRKA receptor binding / transmembrane receptor protein tyrosine kinase adaptor activity / alpha-beta T cell receptor complex ...regulation of superoxide metabolic process / positive regulation of cell proliferation in bone marrow / gamma-delta T cell receptor complex / Fc-gamma receptor III complex / gamma-delta T cell activation / Fc-gamma receptor signaling pathway / XBP1(S) activates chaperone genes / neurotrophin TRKA receptor binding / transmembrane receptor protein tyrosine kinase adaptor activity / alpha-beta T cell receptor complex / positive regulation of protein localization to cell surface / Interleukin-15 signaling / Nef and signal transduction / Interleukin-2 signaling / Signaling by LTK / Shc-EGFR complex / epidermal growth factor receptor binding / epidermal growth factor binding / Signaling by ALK / T cell receptor complex / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / protein complex oligomerization / alpha-beta T cell activation / RET signaling / Generation of second messenger molecules / FCGR activation / Interleukin-3, Interleukin-5 and GM-CSF signaling / Co-inhibition by PD-1 / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / SHC1 events in ERBB4 signaling / Role of LAT2/NTAL/LAB on calcium mobilization / Interleukin receptor SHC signaling / Signalling to RAS / Role of phospholipids in phagocytosis / Signal attenuation / SHC-related events triggered by IGF1R / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / Erythropoietin activates RAS / SHC-mediated cascade:FGFR1 / Signaling by CSF3 (G-CSF) / Tie2 Signaling / insulin-like growth factor receptor binding / ephrin receptor binding / phosphotyrosine residue binding / SHC1 events in EGFR signaling / Integrin signaling / FCERI mediated Ca+2 mobilization / SHC1 events in ERBB2 signaling / Insulin receptor signalling cascade / FCGR3A-mediated IL10 synthesis / insulin-like growth factor receptor signaling pathway / protein tyrosine kinase binding / Constitutive Signaling by Overexpressed ERBB2 / negative regulation of angiogenesis / insulin receptor binding / FCGR3A-mediated phagocytosis / FCERI mediated MAPK activation / Signaling by ERBB2 TMD/JMD mutants / Constitutive Signaling by EGFRvIII / cell-cell adhesion / Signaling by ERBB2 ECD mutants / receptor tyrosine kinase binding / Signaling by ERBB2 KD Mutants / phospholipid binding / Regulation of actin dynamics for phagocytic cup formation / cellular response to growth factor stimulus / Signaling by CSF1 (M-CSF) in myeloid cells / epidermal growth factor receptor signaling pathway / Signaling by ALK fusions and activated point mutants / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Downstream TCR signaling / transmembrane signaling receptor activity / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / insulin receptor signaling pathway / GPER1 signaling / DAP12 signaling / T cell receptor signaling pathway / heart development / actin cytoskeleton organization / RAF/MAP kinase cascade / protein-containing complex assembly / angiogenesis / adaptive immune response / Extra-nuclear estrogen signaling / cell surface receptor signaling pathway / positive regulation of ERK1 and ERK2 cascade / positive regulation of MAPK cascade / intracellular signal transduction / defense response to bacterium / mitochondrial matrix / protein heterodimerization activity / focal adhesion / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / negative regulation of apoptotic process
Similarity search - Function
Phosphotyrosine interaction domain, Shc-like / SH2 adaptor protein C, SH2 domain / : / T-cell surface glycoprotein CD3 zeta subunit / T-cell surface glycoprotein CD3 zeta subunit/High affinity IgE receptor gamma subunit / T-cell surface glycoprotein CD3 zeta chain / Immunoreceptor tyrosine-based activation motif / Phosphorylated immunoreceptor signalling ITAM / ITAM motif mammalian type profile. / Immunoreceptor tyrosine-based activation motif ...Phosphotyrosine interaction domain, Shc-like / SH2 adaptor protein C, SH2 domain / : / T-cell surface glycoprotein CD3 zeta subunit / T-cell surface glycoprotein CD3 zeta subunit/High affinity IgE receptor gamma subunit / T-cell surface glycoprotein CD3 zeta chain / Immunoreceptor tyrosine-based activation motif / Phosphorylated immunoreceptor signalling ITAM / ITAM motif mammalian type profile. / Immunoreceptor tyrosine-based activation motif / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI domain / SH2 domain / SHC Adaptor Protein / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / PH-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
T-cell surface glycoprotein CD3 zeta chain / SHC-transforming protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsZhou, M.-M. / Meadows, R.P. / Logan, T.M. / Yoon, H.S. / Wade, W.R. / Ravichandran, K.S. / Burakoff, S.J. / Feisk, S.W.
Citation
Journal: Proc.Natl.Acad.Sci.USA / Year: 1995
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: Journal: Cell(Cambridge,Mass.) / Year: 1994
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: 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.
#3: 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.
History
DepositionMar 27, 1996Processing site: BNL
Revision 1.0May 15, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details
Revision 1.4Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: SHC
B: PHOSPHOPEPTIDE OF THE ZETA CHAIN OF T CELL RECEPTOR


Theoretical massNumber of molelcules
Total (without water)13,6532
Polymers13,6532
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein SHC


Mass: 12123.677 Da / Num. of mol.: 1 / Fragment: SH2 DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Strain: BL21 (DE3) / Cell line: BL21 / Gene: SH2 DOMAIN OF SHC / Plasmid: PET20B / Gene (production host): SH2 DOMAIN OF SHC / Production host: Escherichia coli (E. coli) / References: UniProt: P29353
#2: Protein/peptide PHOSPHOPEPTIDE OF THE ZETA CHAIN OF T CELL RECEPTOR


Mass: 1529.545 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
References: UniProt: P20963
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR / Developer: BRUNGER / Classification: refinement
RefinementSoftware ordinal: 1
Details: SET OF IDEAL BOND LENGTHS AND ANGLES USED DURING REFINEMENT: PARALLHDG.PRO IN X-PLOR.
NMR ensembleConformers submitted total number: 1

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