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Growth factor PDB id
1tfg
Jmol
Contents
Protein chain
112 a.a. *
Waters ×84
* Residue conservation analysis
PDB id:
1tfg
Name: Growth factor
Title: An unusual feature revealed by the crystal structure at 2.2 resolution of human transforming growth factor-beta2
Structure: Transforming growth factor, beta 2. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Biol. unit: Dimer (from PQS)
Resolution:
1.95Å     R-factor:   0.194    
Authors: M.Gruetter,M.Schlunegger
Key ref: M.P.Schlunegger and M.G.Grütter (1992). An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2. Nature, 358, 430-434. PubMed id: 1641027 DOI: 10.1038/358430a0
Date:
17-Nov-92     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61812  (TGFB2_HUMAN) -  Transforming growth factor beta-2
Seq:
Struc: 		414 a.a.
112 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     growth factor activity     1 term  

 

 
DOI no: 10.1038/358430a0 Nature 358:430-434 (1992)
PubMed id: 1641027  
 
 
An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2.
M.P.Schlunegger, M.G.Grütter.
 
  ABSTRACT  
 
Transforming growth factor type beta 2 (TGF-beta 2) is a member of an expanding family of growth factors that regulate proliferation and differentiation of many different cell types. TGF-beta 2 binds to various receptors, one of which was shown to be a serine/threonine kinase. TGF-beta 2 is involved in wound healing, bone formation and modulation of immune functions. We report here the crystal structure of TGF-beta 2 at 2.2 A resolution, which reveals a novel monomer fold and dimer association. The monomer consists of two antiparallel pairs of beta-strands forming a flat curved surface and a separate, long alpha-helix. The disulphide-rich core has one disulphide bone pointing through a ring formed by the sequence motifs Cys-Ala-Gly-Ala-Cys and Cys-Lys-Cys, which are themselves connected through the cysteines. Two monomers are connected through a single disulphide bridge and associate such that the helix of one subunit interacts with the concave beta-sheet surface of the other. Four exposed loop regions might determine receptor specificity. The structure provides a suitable model for the TGF-beta s and other members of the super-family and is the basis for the analysis of the TGF-beta 2 interactions with the receptor.
 

Literature references that cite this PDB file's key reference

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PDB code: 2k8p
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PDB codes: 1nys 1nyu
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PDB code: 1m9z
12357473 D.B.Everman, C.F.Bartels, Y.Yang, N.Yanamandra, F.R.Goodman, J.R.Mendoza-Londono, R.Savarirayan, S.M.White, J.M.Graham, R.P.Gale, E.Svarch, W.G.Newman, A.R.Kleckers, C.A.Francomano, V.Govindaiah, L.Singh, S.Morrison, J.T.Thomas, and M.L.Warman (2002).
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PDB code: 1ktz
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TGF-beta signal transduction.
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Origin of dimeric structure in the ribonuclease superfamily.
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9726969 N.Beglova, L.LeSauteur, I.Ekiel, H.U.Saragovi, and K.Gehring (1998).
Solution structure and internal motion of a bioactive peptide derived from nerve growth factor.
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9478918 S.S.Huang, and J.S.Huang (1998).
A pentacosapeptide (CKS-25) homologous to retroviral envelope proteins possesses a transforming growth factor-beta activity.
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9748282 S.S.Huang, M.A.Cerullo, F.W.Huang, and J.S.Huang (1998).
Activated thyroglobulin possesses a transforming growth factor-beta activity.
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9356471 A.C.McPherron, and S.J.Lee (1997).
Double muscling in cattle due to mutations in the myostatin gene.
  Proc Natl Acad Sci U S A, 94, 12457-12461.  
9187648 C.Eigenbrot, and N.Gerber (1997).
X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding.
  Nat Struct Biol, 4, 435-438.
PDB code: 1agq
9150447 J.S.Munger, J.G.Harpel, P.E.Gleizes, R.Mazzieri, I.Nunes, and D.B.Rifkin (1997).
Latent transforming growth factor-beta: structural features and mechanisms of activation.
  Kidney Int, 51, 1376-1382.  
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The interaction of the transforming growth factor-betas with heparin/heparan sulfate is isoform-specific.
  J Biol Chem, 272, 18000-18006.  
  9071596 P.C.Marker, K.Seung, A.E.Bland, L.B.Russell, and D.M.Kingsley (1997).
Spectrum of Bmp5 mutations from germline mutagenesis experiments in mice.
  Genetics, 145, 435-443.  
  9170210 P.E.Gleizes, J.S.Munger, I.Nunes, J.G.Harpel, R.Mazzieri, I.Noguera, and D.B.Rifkin (1997).
TGF-beta latency: biological significance and mechanisms of activation.
  Stem Cells, 15, 190-197.  
9395284 R.Derynck, and X.H.Feng (1997).
TGF-beta receptor signaling.
  Biochim Biophys Acta, 1333, F105-F150.  
  9071585 S.J.Newfeld, R.W.Padgett, S.D.Findley, B.G.Richter, M.Sanicola, M.de Cuevas, and W.M.Gelbart (1997).
Molecular evolution at the decapentaplegic locus in Drosophila.
  Genetics, 145, 297-309.  
  11725095 D.H.Kim, and S.J.Kim (1996).
Transforming Growth Factor-beta Receptors: Role in Physiology and Disease.
  J Biomed Sci, 3, 143-158.  
8570652 D.L.Griffith, P.C.Keck, T.K.Sampath, D.C.Rueger, and W.D.Carlson (1996).
Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily.
  Proc Natl Acad Sci U S A, 93, 878-883.
PDB code: 1bmp
8917430 J.F.Goetschy, O.Letourneur, N.Cerletti, and M.A.Horisberger (1996).
The unglycosylated extracellular domain of type-II receptor for transforming growth factor-beta. A novel assay for characterizing ligand affinity and specificity.
  Eur J Biochem, 241, 355-362.  
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Association of the small latent transforming growth factor-beta with an eight cysteine repeat of its binding protein LTBP-1.
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Regulation and interactions of transforming growth factor-beta with cardiovascular cells: implications for development and disease.
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Three-dimensional structures of gonadotropins.
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Molecular lesions associated with alleles of decapentaplegic identify residues necessary for TGF-beta/BMP cell signaling in Drosophila melanogaster.
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Glial cell line-derived neurotrophic factor: selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure.
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  8819159 P.R.Mittl, J.P.Priestle, D.A.Cox, G.McMaster, N.Cerletti, and M.G.Grütter (1996).
The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding.
  Protein Sci, 5, 1261-1271.
PDB codes: 1tgj 1tgk
8620887 R.Ruppert, E.Hoffmann, and W.Sebald (1996).
Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity.
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Interaction of recombinant human bone morphogenetic protein-2 with poly(d,l lactide-co-glycolide) microspheres.
  Pharm Dev Technol, 1, 11-19.  
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Engineering, expression and renaturation of targeted TGF-beta fusion proteins.
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Complex flexibility of the transforming growth factor beta superfamily.
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The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands.
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Cystine knots.
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Transforming growth factor beta and cancer.
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PDB code: 1hcn
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Latent transforming growth factor-beta 1 associates to fibroblast extracellular matrix via latent TGF-beta binding protein.
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TGF-beta related genes in development.
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An extended surface of binding to Trk tyrosine kinase receptors in NGF and BDNF allows the engineering of a multifunctional pan-neurotrophin.
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Receptors for the TGF-beta superfamily: multiple polypeptides and serine/threonine kinases.
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Topological similarities in TGF-beta 2, PDGF-BB and NGF define a superfamily of polypeptide growth factors.
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A structural superfamily of growth factors containing a cystine knot motif.
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The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.