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- PDB-1kld: SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 18-33 OF 33 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1kld
TitleSOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 18-33 OF 33 STRUCTURES
ComponentsTRANSFORMING GROWTH FACTOR-BETA 1
KeywordsGROWTH FACTOR / MITOGEN / GLYCOPROTEIN
Function / homology
Function and homology information


frontal suture morphogenesis / Influenza Virus Induced Apoptosis / adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains / positive regulation of microglia differentiation / regulation of interleukin-23 production / positive regulation of primary miRNA processing / morphogenesis of a branching structure / negative regulation of skeletal muscle tissue development / regulation of striated muscle tissue development / response to laminar fluid shear stress ...frontal suture morphogenesis / Influenza Virus Induced Apoptosis / adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains / positive regulation of microglia differentiation / regulation of interleukin-23 production / positive regulation of primary miRNA processing / morphogenesis of a branching structure / negative regulation of skeletal muscle tissue development / regulation of striated muscle tissue development / response to laminar fluid shear stress / embryonic liver development / heart valve morphogenesis / macrophage derived foam cell differentiation / TGFBR2 MSI Frameshift Mutants in Cancer / regulation of protein import into nucleus / regulation of blood vessel remodeling / transforming growth factor beta complex / cellular response to acetaldehyde / negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of macrophage cytokine production / extracellular matrix assembly / negative regulation of hyaluronan biosynthetic process / connective tissue replacement involved in inflammatory response wound healing / type III transforming growth factor beta receptor binding / myofibroblast differentiation / TGFBR2 Kinase Domain Mutants in Cancer / positive regulation of exit from mitosis / positive regulation of isotype switching to IgA isotypes / SMAD2/3 Phosphorylation Motif Mutants in Cancer / TGFBR1 KD Mutants in Cancer / odontoblast differentiation / positive regulation of mesenchymal stem cell proliferation / positive regulation of receptor signaling pathway via STAT / membrane protein intracellular domain proteolysis / positive regulation of extracellular matrix assembly / negative regulation of myoblast differentiation / TGFBR3 regulates TGF-beta signaling / positive regulation of vasculature development / hyaluronan catabolic process / ATP biosynthetic process / negative regulation of extracellular matrix disassembly / type II transforming growth factor beta receptor binding / cell-cell junction organization / positive regulation of branching involved in ureteric bud morphogenesis / receptor catabolic process / positive regulation of cardiac muscle cell differentiation / response to salt / TGFBR1 LBD Mutants in Cancer / regulatory T cell differentiation / positive regulation of chemotaxis / negative regulation of cell-cell adhesion mediated by cadherin / negative regulation of biomineral tissue development / type I transforming growth factor beta receptor binding / positive regulation of vascular permeability / positive regulation of mononuclear cell migration / ureteric bud development / oligodendrocyte development / negative regulation of interleukin-17 production / phosphate-containing compound metabolic process / face morphogenesis / sprouting angiogenesis / response to cholesterol / digestive tract development / neural tube development / odontogenesis of dentin-containing tooth / positive regulation of chemokine (C-X-C motif) ligand 2 production / response to vitamin D / positive regulation of fibroblast migration / aortic valve morphogenesis / RUNX3 regulates CDKN1A transcription / negative regulation of release of sequestered calcium ion into cytosol / negative regulation of fat cell differentiation / positive regulation of regulatory T cell differentiation / Molecules associated with elastic fibres / negative regulation of neuroblast proliferation / Syndecan interactions / cellular response to insulin-like growth factor stimulus / inner ear development / negative regulation of phagocytosis / ventricular cardiac muscle tissue morphogenesis / positive regulation of interleukin-17 production / response to immobilization stress / cellular response to dexamethasone stimulus / negative regulation of cell cycle / chondrocyte differentiation / positive regulation of collagen biosynthetic process / TGF-beta receptor signaling activates SMADs / positive regulation of protein metabolic process / hematopoietic progenitor cell differentiation / negative regulation of blood vessel endothelial cell migration / positive regulation of cell division / positive regulation of SMAD protein signal transduction / epithelial to mesenchymal transition / vasculogenesis / lymph node development / positive regulation of endothelial cell apoptotic process / positive regulation of vascular endothelial growth factor production / defense response to fungus / RUNX3 regulates p14-ARF / cellular response to low-density lipoprotein particle stimulus
Similarity search - Function
Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Cystine Knot Cytokines, subunit B / Cystine-knot cytokines ...Transforming growth factor beta-1 proprotein / Transforming growth factor-beta / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Transforming growth factor-beta-related / Transforming growth factor-beta (TGF-beta) family / Cystine Knot Cytokines, subunit B / Cystine-knot cytokines / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Cystine-knot cytokine / Ribbon / Mainly Beta
Similarity search - Domain/homology
Transforming growth factor beta-1 proprotein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsHinck, A.P. / Archer, S.J. / Qian, S.W. / Roberts, A.B. / Sporn, M.B. / Weatherbee, J.A. / Tsang, M.L.-S. / Lucas, R. / Zhang, B.-L. / Wenker, J. / Torchia, D.A.
CitationJournal: Biochemistry / Year: 1996
Title: Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2.
Authors: Hinck, A.P. / Archer, S.J. / Qian, S.W. / Roberts, A.B. / Sporn, M.B. / Weatherbee, J.A. / Tsang, M.L. / Lucas, R. / Zhang, B.L. / Wenker, J. / Torchia, D.A.
History
DepositionJan 16, 1996Processing site: BNL
Revision 1.0Aug 17, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: TRANSFORMING GROWTH FACTOR-BETA 1
B: TRANSFORMING GROWTH FACTOR-BETA 1


Theoretical massNumber of molelcules
Total (without water)25,6202
Polymers25,6202
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)16 / 33
Representative

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Components

#1: Protein TRANSFORMING GROWTH FACTOR-BETA 1 / TGF-B1


Mass: 12809.812 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: 1 MM (IN DIMER), PH 4.2 / Source: (gene. exp.) Homo sapiens (human) / Organ: OVARY / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P01137
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: THIS ENTRY CONTAINS 18 - 33 OF 33 MODELS. 1 MM (IN DIMER).

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Sample preparation

Sample conditionspH: 4.2 / Temperature units: K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
XPLOR3.1structure solution
NMR ensembleConformers calculated total number: 33 / Conformers submitted total number: 16

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