TGF-beta receptor

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (03:19, 2 October 2022) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='1ktz' size='340' side='right' caption='Human hTGFBR-II extracellular domain (green) complex with TGF-β3 (grey) (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=''>
__TOC__
__TOC__
== Function ==
== Function ==
-
'''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<ref>PMID:9525694</ref>. There are 3 types of TGFBR: <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 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. TGFBR I has high affinity for TGF-β1 and low affinity for TGF-β2. <br />
+
*'''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 />
-
*'''TGFBR II''' is a tumor suppressor transmembrane protein. TGFBR II 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 />
-
*'''TGFBR III''' is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan. It acts as a reservoir of ligand for TGFBRs. TGFBR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2.
+
*'''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 ==
== Disease ==
-
Over-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFBR II cause various types of tumors<ref>PMID:23884466</ref>.
+
Over-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFR II cause various types of tumors<ref>PMID:23884466</ref>.
== Structural highlights ==
== Structural highlights ==
-
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.
+
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]]
</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]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

References

  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky

Retrieved from "http://52.214.119.220/wiki/index.php/TGF-beta_receptor"
Personal tools