TGF-beta receptor: Difference between revisions

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<StructureSection load='1ktz' size='340' side='right' caption='Human hTGFBR-II extracellular domain complex with TGF-β3 (PDB code [[1ktz]])' scene=''>
<StructureSection load='1ktz' size='340' side='right' caption='Human hTGFR-II extracellular domain (green) complex with TGF-β3 (grey) (PDB code [[1ktz]])' scene=''>
'''TGF-β receptors''' (Transforming Growth Factor) (TGFBR) are serine/threonine kinase receptors.  They are involved in paracrine signaling and are found in many types of tissue.  TGF-β ligands include bone morphogenetic proteins, growth and initiation factors, anti-Mullerian hormone, activin, nodal TGF-β. TGFBR structure contains a 100-140 residues ligand-binding N-terminal extracellular domain; a transmembrane domain;  a 350-400 amino acid cytoplasmic kinase domain; and a C-terminal zona pellucida (ZP) domain of ca 260 residues which has a role in protein polymerization..  There are 3 types of TGFBR.  Both TGFBR I and II have high affinity for TGF-β1 and low affinity for TGF-β2.  TGFBR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2. <br />
__TOC__
*'''TGFBR I''' forms heteromeric complex with TGFBR II when it is bound to TGF-β.  The complex transduces the TGF-β signal from the cell surface to the cytoplasm by phosphorylating proteins which regulate the transcription of genes related to cell proliferation.<br />   
== Function ==
*'''TGFBR II''' is a tumor suppressor transmembrane protein.  <br />
'''TGF-β receptors''' (Transforming Growth Factor) (TGFR) are [[serine/threonine kinase]] receptors.  They are involved in paracrine signaling and are found in many types of tissue.  TGF-β ligands include bone morphogenetic proteins, growth and initiation factors, anti-Mullerian hormone, activin, nodal TGF-β<ref>PMID:9525694</ref>.   There are 3 types of TGFR:    <br />
*'''TGFBR III''' is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan.  It acts as a reservoir of ligand for TGFBRs.
*'''TGFR I''' forms heteromeric complex with TGFR II when it is bound to TGF-β.  The complex transduces the TGF-β signal from the cell surface to the cytoplasm by phosphorylating proteins which regulate the transcription of genes related to cell proliferation.  TGFR I has high affinity for TGF-β1 and low affinity for TGF-β2. <br />   
 
*'''TGFR II''' is a tumor suppressor transmembrane protein.  TGFR II has high affinity for TGF-β1 and low affinity for TGF-β2. <br />
*'''TGFR III''' is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan.  It acts as a reservoir of ligand for TGFRs.  TGFR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2.


== Function ==
See also [[Receptor]], [[TGF beta signaling pathway]], and [[Growth factors]].


== Disease ==
== Disease ==


Over-expression of TGF causes kidney disease, diabetes and renal disease.  Mutations in TGFBR II cause various types of tumors.
Over-expression of TGF causes kidney disease, diabetes and renal disease.  Mutations in TGFR II cause various types of tumors<ref>PMID:23884466</ref>.


== Relevance ==
== Structural highlights ==
TGFR structure contains a 100-140 residues ligand-binding N-terminal extracellular domain; a transmembrane domain;  a 350-400 amino acid cytoplasmic kinase domain; and a C-terminal zona pellucida (ZP) domain of ca 260 residues which has a role in protein polymerization.


== Structural highlights ==
== 3D Structures of TGF-beta receptor==
[[TGF-beta receptor 3D structures]]


</StructureSection>
</StructureSection>


== 3D Structures of TGF-β receptor==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
* TGF-β receptor I
**[[1ias]] – hTGFBR-I kinase domain – human  <br />
**[[2l5s]] – hTGFBR-I extracellular domain - NMR<br />
**[[1b6c]] – hTGFBR-I kinase domain + FKBP12 <br />
**[[1py5]], [[3faa]], [[3gxl]], [[3hmm]], [[2wot]], [[2wou]], [[3kcf]], [[2x7o]], [[3tzm]], [[4x0m]], [[4x2j]], [[4x2k]], [[4x2n]] – hTGFBR-I kinase domain + inhibitor  <br />
**[[1vjy]] – hTGFBR-I residues 1-303 + inhibitor  <br />
**[[1rw8]] – hTGFBR-I truncated kinase domain + inhibitor  <br />
* TGF-β receptor II
**[[1m9z]] – hTGFBR-II extracellular domain <br />
**[[1plo]], [[4p7u]] – hTGFBR-II extracellular domain (mutant) - NMR<br />
**[[1ks6]] – cTGFBR-II extracellular domain - chicken<br />
**[[1ktz]] – hTGFBR-II extracellular domain + TGF-β3  <br />
* TGF-β receptor III
**[[3qw9]] – TGFBR-III ZP-C domain - rat<br />
**[[4ajv]] – TGFBR-III ZP-C domain - mouse<br />
* TGF-β receptor I+II
**[[2pjy]] – hTGFBR-I extracellular domain (mutant) +  hTGFBR-II extracellular domain (mutant) + TGF-β3  <br />
**[[3kfd]] – hTGFBR-I extracellular domain +  hTGFBR-II extracellular domain + TGF-β1  <br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

Latest revision as of 06:19, 2 October 2022

Function

TGF-β receptors (Transforming Growth Factor) (TGFR) are serine/threonine kinase receptors. They are involved in paracrine signaling and are found in many types of tissue. TGF-β ligands include bone morphogenetic proteins, growth and initiation factors, anti-Mullerian hormone, activin, nodal TGF-β[1]. There are 3 types of TGFR:

  • TGFR I forms heteromeric complex with TGFR II when it is bound to TGF-β. The complex transduces the TGF-β signal from the cell surface to the cytoplasm by phosphorylating proteins which regulate the transcription of genes related to cell proliferation. TGFR I has high affinity for TGF-β1 and low affinity for TGF-β2.
  • TGFR II is a tumor suppressor transmembrane protein. TGFR II has high affinity for TGF-β1 and low affinity for TGF-β2.
  • TGFR III is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan. It acts as a reservoir of ligand for TGFRs. TGFR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2.

See also Receptor, TGF beta signaling pathway, and Growth factors.

Disease

Over-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFR II cause various types of tumors[2].

Structural highlights

TGFR structure contains a 100-140 residues ligand-binding N-terminal extracellular domain; a transmembrane domain; a 350-400 amino acid cytoplasmic kinase domain; and a C-terminal zona pellucida (ZP) domain of ca 260 residues which has a role in protein polymerization.

3D Structures of TGF-beta receptor

TGF-beta receptor 3D structures


Human hTGFR-II extracellular domain (green) complex with TGF-β3 (grey) (PDB code 1ktz)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Wrana JL. TGF-beta receptors and signalling mechanisms. Miner Electrolyte Metab. 1998;24(2-3):120-30. PMID:9525694
  2. ↑ Frischmeyer-Guerrerio PA, Guerrerio AL, Oswald G, Chichester K, Myers L, Halushka MK, Oliva-Hemker M, Wood RA, Dietz HC. TGFbeta receptor mutations impose a strong predisposition for human allergic disease. Sci Transl Med. 2013 Jul 24;5(195):195ra94. doi: 10.1126/scitranslmed.3006448. PMID:23884466 doi:http://dx.doi.org/10.1126/scitranslmed.3006448

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