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- PDB-2met: NMR spatial structure of the trimeric mutant TM domain of VEGFR2 ... -

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Basic information

Entry
Database: PDB / ID: 2met
TitleNMR spatial structure of the trimeric mutant TM domain of VEGFR2 receptor.
ComponentsVascular endothelial growth factor receptor 2
KeywordsSIGNALING PROTEIN / VEGFR / receptor tyrosine kinase / homodimer
Function / homology
Function and homology information


positive regulation of nitric oxide-cGMP mediated signal transduction / blood vessel endothelial cell differentiation / regulation of bone development / cellular response to hydrogen sulfide / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / Neuropilin interactions with VEGF and VEGFR / vascular endothelial growth factor binding / vascular endothelial growth factor receptor-2 signaling pathway / VEGF binds to VEGFR leading to receptor dimerization / endocardium development ...positive regulation of nitric oxide-cGMP mediated signal transduction / blood vessel endothelial cell differentiation / regulation of bone development / cellular response to hydrogen sulfide / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / Neuropilin interactions with VEGF and VEGFR / vascular endothelial growth factor binding / vascular endothelial growth factor receptor-2 signaling pathway / VEGF binds to VEGFR leading to receptor dimerization / endocardium development / endothelium development / regulation of hematopoietic progenitor cell differentiation / vascular endothelial growth factor receptor activity / mesenchymal cell proliferation / post-embryonic camera-type eye morphogenesis / endothelial cell differentiation / lymph vessel development / positive regulation of vasculogenesis / vascular wound healing / positive regulation of BMP signaling pathway / surfactant homeostasis / epithelial cell maturation / anchoring junction / positive regulation of positive chemotaxis / positive regulation of endothelial cell chemotaxis / embryonic hemopoiesis / positive regulation of mesenchymal cell proliferation / positive regulation of cell migration involved in sprouting angiogenesis / vascular endothelial growth factor signaling pathway / lung alveolus development / positive regulation of mitochondrial fission / branching involved in blood vessel morphogenesis / growth factor binding / positive regulation of stem cell proliferation / sorting endosome / positive regulation of mitochondrial depolarization / semaphorin-plexin signaling pathway / regulation of MAPK cascade / positive regulation of macroautophagy / cellular response to vascular endothelial growth factor stimulus / positive regulation of focal adhesion assembly / positive regulation of blood vessel endothelial cell migration / vascular endothelial growth factor receptor signaling pathway / cell fate commitment / Integrin cell surface interactions / negative regulation of endothelial cell apoptotic process / vasculogenesis / ovarian follicle development / coreceptor activity / calcium ion homeostasis / peptidyl-tyrosine phosphorylation / positive regulation of endothelial cell proliferation / transmembrane receptor protein tyrosine kinase activity / positive regulation of endothelial cell migration / epithelial cell proliferation / cell surface receptor protein tyrosine kinase signaling pathway / stem cell proliferation / VEGFR2 mediated cell proliferation / receptor protein-tyrosine kinase / Hsp90 protein binding / positive regulation of protein phosphorylation / VEGFA-VEGFR2 Pathway / integrin binding / positive regulation of angiogenesis / cell junction / protein autophosphorylation / regulation of cell shape / cell migration / protein tyrosine kinase activity / angiogenesis / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / negative regulation of neuron apoptotic process / early endosome / positive regulation of ERK1 and ERK2 cascade / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / signaling receptor complex / endosome / positive regulation of cell migration / cadherin binding / membrane raft / external side of plasma membrane / negative regulation of gene expression / positive regulation of cell population proliferation / endoplasmic reticulum / Golgi apparatus / extracellular region / ATP binding / identical protein binding / nucleus / plasma membrane
Similarity search - Function
Vascular endothelial growth factor receptor 2 (VEGFR2) / VEGFR-2, transmembrane domain / : / : / VEGFR-2 Transmembrane domain / Vascular endothelial growth factor receptor 1-like, Ig-like domain / VEGFR1-3, N-terminal Ig-like domain / VEGFR-1-like, immunoglobulin-like domain / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. ...Vascular endothelial growth factor receptor 2 (VEGFR2) / VEGFR-2, transmembrane domain / : / : / VEGFR-2 Transmembrane domain / Vascular endothelial growth factor receptor 1-like, Ig-like domain / VEGFR1-3, N-terminal Ig-like domain / VEGFR-1-like, immunoglobulin-like domain / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. / Immunoglobulin domain / Immunoglobulin / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / : / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Immunoglobulin subtype / Immunoglobulin / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / 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
Similarity search - Domain/homology
Vascular endothelial growth factor receptor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
Model detailsfewest violations, model1
AuthorsMineev, K.S. / Arseniev, A.A. / Shulepko, M. / Lyukmanova, E.N. / Kirpichnikov, M.P.
CitationJournal: Structure / Year: 2014
Title: Structural and functional characterization of alternative transmembrane domain conformations in VEGF receptor 2 activation
Authors: Manni, S. / Mineev, K.S. / Usmanova, D. / Lyukmanova, E.N. / Shulepko, M.A. / Kirpichnikov, M.P. / Winter, J. / Matkovic, M. / Deupi, X. / Arseniev, A.S. / Ballmer-Hofer, K.
History
DepositionOct 2, 2013Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Jul 30, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 6, 2017Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / 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.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.3May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Vascular endothelial growth factor receptor 2
B: Vascular endothelial growth factor receptor 2
C: Vascular endothelial growth factor receptor 2


Theoretical massNumber of molelcules
Total (without water)12,4833
Polymers12,4833
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)10 / 100target function
RepresentativeModel #1fewest violations

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Components

#1: Protein/peptide Vascular endothelial growth factor receptor 2 / VEGFR-2 / Fetal liver kinase 1 / FLK-1 / Kinase insert domain receptor / KDR / Protein-tyrosine ...VEGFR-2 / Fetal liver kinase 1 / FLK-1 / Kinase insert domain receptor / KDR / Protein-tyrosine kinase receptor flk-1


Mass: 4161.049 Da / Num. of mol.: 3 / Fragment: UNP residues 759-795 / Mutation: V11E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KDR, FLK1, VEGFR2 / Production host: Escherichia coli (E. coli)
References: UniProt: P35968, receptor protein-tyrosine kinase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
Details: The TM domain of VEGRF2 bears the V/E substitution at the position 769.
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-13C HSQC
1313D CBCA(CO)NH
1413D HN(CA)CB
1513D HNCA
1613D HNCO
1713D 1H-13C NOESY aliphatic
1813D 1H-13C NOESY aromatic
1913D 1H-15N NOESY
110113C,15N - filtered NOESY-HSQC

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Sample preparation

DetailsContents: 0.6mM VEGFR-2tm769-1, 0.6mM [U-100% 13C; U-100% 15N] VEGFR-2tm769-2, 120mM [U-100% 2H] DPC-3, 20mM [U-99% 2H] sodium acetate-4, 3mM sodium azide-5, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.6 mMVEGFR-2tm769-11
0.6 mMVEGFR-2tm769-2[U-100% 13C; U-100% 15N]1
120 mMDPC-3[U-100% 2H]1
20 mMsodium acetate-4[U-99% 2H]1
3 mMsodium azide-51
Sample conditionsIonic strength: 20 / pH: 4.5 / Pressure: ambient atm / Temperature: 318 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CYANA3Guntert, Mumenthaler and Wuthrichstructure solution
CARA1.8.4Keller and Wuthrichchemical shift assignment
CARA1.8.4Keller and Wuthrichdata analysis
TopSpin3Bruker Biospincollection
qMDD2.1Orekhov, Mayzelprocessing
CYANArefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 10 / Representative conformer: 1

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