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- PDB-1shc: SHC PTB DOMAIN COMPLEXED WITH A TRKA RECEPTOR PHOSPHOPEPTIDE, NMR... -

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Basic information

Entry
Database: PDB / ID: 1shc
TitleSHC PTB DOMAIN COMPLEXED WITH A TRKA RECEPTOR PHOSPHOPEPTIDE, NMR, MINIMIZED AVERAGE STRUCTURE
Components
  • SHC
  • TRKA RECEPTOR PHOSPHOPEPTIDE
KeywordsCOMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) / PHOSPHOTYROSINE BINDING DOMAIN (PTB) / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) complex
Function / homology
Function and homology information


regulation of superoxide metabolic process / positive regulation of cell proliferation in bone marrow / neurotrophin p75 receptor binding / behavioral response to formalin induced pain / olfactory nerve development / response to hydrostatic pressure / TRKA activation by NGF / PLC-gamma1 signalling / Signalling to STAT3 / neurotrophin receptor activity ...regulation of superoxide metabolic process / positive regulation of cell proliferation in bone marrow / neurotrophin p75 receptor binding / behavioral response to formalin induced pain / olfactory nerve development / response to hydrostatic pressure / TRKA activation by NGF / PLC-gamma1 signalling / Signalling to STAT3 / neurotrophin receptor activity / programmed cell death involved in cell development / mechanoreceptor differentiation / nerve growth factor receptor activity / neurotrophin binding / nerve growth factor signaling pathway / axonogenesis involved in innervation / Sertoli cell development / Retrograde neurotrophin signalling / nerve growth factor binding / XBP1(S) activates chaperone genes / sympathetic nervous system development / NGF-independant TRKA activation / Signalling to p38 via RIT and RIN / neurotrophin TRKA receptor binding / ARMS-mediated activation / transmembrane receptor protein tyrosine kinase adaptor activity / Interleukin-15 signaling / positive regulation of programmed cell death / positive regulation of Ras protein signal transduction / positive regulation of synapse assembly / Interleukin-2 signaling / Signaling by LTK / PI3K/AKT activation / Shc-EGFR complex / epidermal growth factor receptor binding / epidermal growth factor binding / Signaling by ALK / Frs2-mediated activation / neurotrophin TRK receptor signaling pathway / detection of temperature stimulus involved in sensory perception of pain / RET signaling / Interleukin-3, Interleukin-5 and GM-CSF signaling / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / SHC1 events in ERBB4 signaling / Role of LAT2/NTAL/LAB on calcium mobilization / Signalling to RAS / response to axon injury / Interleukin receptor SHC signaling / Signal attenuation / neuron development / SHC-related events triggered by IGF1R / detection of mechanical stimulus involved in sensory perception of pain / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / response to electrical stimulus / SHC-mediated cascade:FGFR2 / peptidyl-tyrosine autophosphorylation / SHC-mediated cascade:FGFR4 / Signaling by CSF3 (G-CSF) / Erythropoietin activates RAS / SHC-mediated cascade:FGFR1 / Tie2 Signaling / insulin-like growth factor receptor binding / ephrin receptor binding / transmembrane receptor protein tyrosine kinase activity / SHC1 events in EGFR signaling / phosphotyrosine residue binding / Integrin signaling / positive regulation of GTPase activity / FCERI mediated Ca+2 mobilization / SHC1 events in ERBB2 signaling / Insulin receptor signalling cascade / B cell differentiation / positive regulation of synaptic transmission, glutamatergic / insulin-like growth factor receptor signaling pathway / axon guidance / Constitutive Signaling by Overexpressed ERBB2 / cell surface receptor protein tyrosine kinase signaling pathway / negative regulation of angiogenesis / FCERI mediated MAPK activation / insulin receptor binding / Signaling by ERBB2 TMD/JMD mutants / cellular response to nerve growth factor stimulus / response to nutrient levels / placental growth factor receptor activity / insulin receptor activity / vascular endothelial growth factor receptor activity / Constitutive Signaling by EGFRvIII / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity
Similarity search - Function
Phosphotyrosine interaction domain, Shc-like / SH2 adaptor protein C, SH2 domain / : / High affinity nerve growth factor receptor NTRK1 / Tyrosine kinase receptor A, transmembrane domain / Tyrosine kinase receptor A trans-membrane domain / Growth factor receptor NTRK / Growth factor receptor NTRK, leucine rich repeat C-terminal / Leucine rich repeat C-terminal motif / Phosphotyrosine interaction domain (PTB/PID) ...Phosphotyrosine interaction domain, Shc-like / SH2 adaptor protein C, SH2 domain / : / High affinity nerve growth factor receptor NTRK1 / Tyrosine kinase receptor A, transmembrane domain / Tyrosine kinase receptor A trans-membrane domain / Growth factor receptor NTRK / Growth factor receptor NTRK, leucine rich repeat C-terminal / Leucine rich repeat C-terminal motif / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI domain / Cysteine-rich flanking region, C-terminal / Leucine rich repeat C-terminal domain / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / Leucine rich repeat / : / Leucine-rich repeat / SH2 domain / Leucine-rich repeat domain superfamily / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / PH-like domain superfamily / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Roll / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Beta
Similarity search - Domain/homology
High affinity nerve growth factor receptor / SHC-transforming protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsZhou, M.-M. / Ravichandran, K.S. / Olejniczak, E.T. / Petros, A.M. / Meadows, R.P. / Sattler, M. / Harlan, J.E. / Wade, W.S. / Burakoff, S.J. / Fesik, S.W.
Citation
Journal: Nature / Year: 1995
Title: Structure and ligand recognition of the phosphotyrosine binding domain of Shc.
Authors: Zhou, M.M. / Ravichandran, K.S. / Olejniczak, E.F. / Petros, A.M. / Meadows, R.P. / Sattler, M. / Harlan, J.E. / Wade, W.S. / Burakoff, S.J. / Fesik, S.W.
#1: Journal: Nat.Struct.Biol. / Year: 1996
Title: Structural Basis for Il-4 Receptor Phosphopeptide Recognition by the Irs-1 Ptb Domain
Authors: Zhou, M.M. / Huang, B. / Olejniczak, E.T. / Meadows, R.P. / Shuker, S.B. / Miyazaki, M. / Trub, T. / Shoelson, S.E. / Fesik, S.W.
#2: Journal: J.Biol.Chem. / Year: 1995
Title: Specificity of the Ptb Domain of Shc for Beta Turn-Forming Pentapeptide Motifs Amino-Terminal to Phosphotyrosine
Authors: Trub, T. / Choi, W.E. / Wolf, G. / Ottinger, E. / Chen, Y. / Weiss, M. / Shoelson, S.E.
#3: Journal: Science / Year: 1994
Title: An Alternative to Sh2 Domains for Binding Tyrosine-Phosphorylated Proteins
Authors: Kavanaugh, W.M. / Williams, L.T.
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:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: SHC
B: TRKA RECEPTOR PHOSPHOPEPTIDE


Theoretical massNumber of molelcules
Total (without water)22,9242
Polymers22,9242
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: 21409.584 Da / Num. of mol.: 1 / Fragment: PTB DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Strain: BL21 (DE3) / Cell line: BL21 / Gene: PTB DOMAIN OF SHC / Plasmid: PET15B / Gene (production host): PTB DOMAIN OF SHC / Production host: Escherichia coli (E. coli) / References: UniProt: P29353
#2: Protein/peptide TRKA RECEPTOR PHOSPHOPEPTIDE


Mass: 1514.508 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
References: UniProt: P04629
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 WERE USED DURING REFINEMENT: PARALLHDG.PRO IN X-PLOR.
NMR ensembleConformers submitted total number: 1

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