Summary: Transforming growth factor beta receptor 2 ectodomain
This is the Wikipedia entry entitled "TGF beta receptor 2". More...
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TGF beta receptor 2 Edit Wikipedia article
|Transforming growth factor, beta receptor II (70/80kDa)|
PDB rendering based on 1ktz.
|Symbols||; AAT3; FAA3; LDS1B; LDS2; LDS2B; MFS2; RIIC; TAAD2; TGFR-2; TGFbeta-RII|
|External IDs||ChEMBL: GeneCards:|
|RNA expression pattern|
This gene encodes a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. The encoded protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in this gene have been associated with Marfan syndrome, Loeys-Deitz aortic aneurysm syndrome, Osler-Weber-Rendu syndrome, and the development of various types of tumors. Alternatively spliced transcript variants encoding different isoforms have been characterized.
TGF beta receptor 2 has been shown to interact with Cyclin B2, TGF beta receptor 1, Transforming growth factor, beta 3, AP2B1, Endoglin, Heat shock protein 90kDa alpha (cytosolic), member A1 and STRAP.
|Transforming growth factor beta receptor 2 ectodomain|
crystal structure of human tgf-beta type ii receptor ligand binding domain
TGF beta receptor 2 consists of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilised by a network of six intra strand disulphide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets (beta1-beta4, beta3-beta9).
- "TGFBR2 - transforming growth factor, beta receptor II (70/80kDa) - Genetics Home Reference". Retrieved 2008-09-07.
- "Entrez Gene: TGFBR2 transforming growth factor, beta receptor II (70/80kDa)".
- Liu, J H; Wei S; Burnette P K; Gamero A M; Hutton M; Djeu J Y (January 1999). "Functional association of TGF-beta receptor II with cyclin B". Oncogene (ENGLAND) 18 (1): 269–75. doi:10.1038/sj.onc.1202263. ISSN 0950-9232. PMID 9926943.
- Kawabata, M; Chytil A; Moses H L (March 1995). "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor". J. Biol. Chem. (UNITED STATES) 270 (10): 5625–30. doi:10.1074/jbc.270.10.5625. ISSN 0021-9258. PMID 7890683.
- Razani, B; Zhang X L; Bitzer M; von Gersdorff G; Böttinger E P; Lisanti M P (March 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". J. Biol. Chem. (United States) 276 (9): 6727–38. doi:10.1074/jbc.M008340200. ISSN 0021-9258. PMID 11102446.
- De Crescenzo, Gregory; Pham Phuong L, Durocher Yves, O'Connor-McCourt Maureen D (May 2003). "Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding". J. Mol. Biol. (England) 328 (5): 1173–83. doi:10.1016/S0022-2836(03)00360-7. ISSN 0022-2836. PMID 12729750.
- Hart, P John; Deep Shashank; Taylor Alexander B; Shu Zhanyong; Hinck Cynthia S; Hinck Andrew P (March 2002). "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex". Nat. Struct. Biol. (United States) 9 (3): 203–8. doi:10.1038/nsb766. ISSN 1072-8368. PMID 11850637.
- Barbara, N P; Wrana J L; Letarte M (January 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". J. Biol. Chem. (UNITED STATES) 274 (2): 584–94. doi:10.1074/jbc.274.2.584. ISSN 0021-9258. PMID 9872992.
- Rotzer, D; Roth M; Lutz M; Lindemann D; Sebald W; Knaus P (February 2001). "Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor". EMBO J. (England) 20 (3): 480–90. doi:10.1093/emboj/20.3.480. ISSN 0261-4189. PMC 133482. PMID 11157754.
- Yao, Diying; Ehrlich Marcelo; Henis Yoav I; Leof Edward B (November 2002). "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Mol. Biol. Cell (United States) 13 (11): 4001–12. doi:10.1091/mbc.02-07-0104. ISSN 1059-1524. PMC 133610. PMID 12429842.
- Guerrero-Esteo, Mercedes; Sanchez-Elsner Tilman, Letamendia Ainhoa, Bernabeu Carmelo (August 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". J. Biol. Chem. (United States) 277 (32): 29197–209. doi:10.1074/jbc.M111991200. ISSN 0021-9258. PMID 12015308.
- Wrighton, Katharine H; Lin Xia; Feng Xin-Hua (July 2008). "Critical regulation of TGFbeta signaling by Hsp90". Proc. Natl. Acad. Sci. U.S.A. (United States) 105 (27): 9244–9. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668.
- Datta, P K; Chytil A; Gorska A E; Moses H L (Dec 1998). "Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling". J. Biol. Chem. (UNITED STATES) 273 (52): 34671–4. doi:10.1074/jbc.273.52.34671. ISSN 0021-9258. PMID 9856985.
- Datta, P K; Moses H L (May 2000). "STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling". Mol. Cell. Biol. (UNITED STATES) 20 (9): 3157–67. doi:10.1128/MCB.20.9.3157-3167.2000. ISSN 0270-7306. PMC 85610. PMID 10757800.
Transforming growth factor beta receptor 2 ectodomain Provide feedback
The Transforming growth factor beta receptor 2 ectodomain is a compact fold consisting of nine beta-strands and a single helix stabilised by a network of six intra strand disulphide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets (beta1-beta4, beta3-beta9) .
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015013
The Transforming growth factor beta receptor 2 ectodomain is a compact fold consisting of nine beta-strands and a single helix stabilised by a network of six intra strand disulphide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets (beta1-beta4, beta3-beta9) [PUBMED:11850637].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
|Molecular function||metal ion binding (GO:0046872)|
|ATP binding (GO:0005524)|
|transforming growth factor beta receptor activity, type II (GO:0005026)|
|Biological process||protein phosphorylation (GO:0006468)|
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Curation and family details
|Author:||Mistry J, Sammut SJ|
|Number in seed:||20|
|Number in full:||137|
|Average length of the domain:||105.00 aa|
|Average identity of full alignment:||55 %|
|Average coverage of the sequence by the domain:||20.82 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
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There are 3 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ecTbetaR2 domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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