TGF-beta receptor

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== 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.
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.
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== 3D Structures of TGF-β receptor==
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[[TGF-β receptor 3D structures]]
</StructureSection>
</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
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* TGF-β receptor I; kinase domain 200-503
+
* TGF-β receptor I; Domains: extracellular 33-112; kinase 200-503
**[[1ias]], [[5e8s]] – hTGFBR-I kinase domain – human <br />
**[[1ias]], [[5e8s]] – hTGFBR-I kinase domain – human <br />
**[[5e8t]], [[5e8u]] – hTGFBR-I kinase domain (mutant) <br />
**[[5e8t]], [[5e8u]] – hTGFBR-I kinase domain (mutant) <br />
**[[5e8w]], [[5e8x]] – hTGFBR-I kinase domain (mutant) + staurosporine<br />
**[[5e8w]], [[5e8x]] – hTGFBR-I kinase domain (mutant) + staurosporine<br />
-
**[[5e8z]] – hTGFBR-I kinase domain (mutant) + inhibitor<br />
 
**[[2l5s]] – hTGFBR-I extracellular domain - NMR<br />
**[[2l5s]] – hTGFBR-I extracellular domain - NMR<br />
**[[1b6c]] – hTGFBR-I kinase domain + FKBP12 <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 />
+
**[[1py5]], [[3faa]], [[3gxl]], [[3hmm]], [[2wot]], [[2wou]], [[3kcf]], [[2x7o]], [[3tzm]], [[4x0m]], [[4x2j]], [[4x2k]], [[4x2n]], [[5qim]], [[5fri]], [[4x2g]], [[4x2f]] – hTGFBR-I kinase domain + inhibitor <br />
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**[[5e8z]], [[5qik]], [[5qil]], [[5qtz]], [[5qu0]], [[6b8y]], [[5e90]] – hTGFBR-I kinase domain (mutant) + inhibitor<br />
**[[1vjy]] – hTGFBR-I residues 1-303 + inhibitor <br />
**[[1vjy]] – hTGFBR-I residues 1-303 + inhibitor <br />
**[[5usq]] – hTGFBR-I residues 123-421 + inhibitor <br />
**[[5usq]] – hTGFBR-I residues 123-421 + inhibitor <br />
**[[1rw8]] – hTGFBR-I truncated kinase domain + inhibitor <br />
**[[1rw8]] – hTGFBR-I truncated kinase domain + inhibitor <br />
 +
**[[6mac]] – hTGFBR-I extracellular domain + GDF-11 + activin receptor 2B- <br />
* TGF-β receptor II
* TGF-β receptor II
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**[[1m9z]] – hTGFBR-II extracellular domain <br />
**[[1m9z]] – hTGFBR-II extracellular domain <br />
**[[1plo]], [[4p7u]] – hTGFBR-II extracellular domain (mutant) - NMR<br />
**[[1plo]], [[4p7u]] – hTGFBR-II extracellular domain (mutant) - NMR<br />
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**[[4xjj]] – hTGFBR-II extracellular domain (mutant) + inhibitor<br />
**[[5e8v]] – hTGFBR-II kinase domain (mutant) <br />
**[[5e8v]] – hTGFBR-II kinase domain (mutant) <br />
**[[5e8y]] – hTGFBR-II kinase domain (mutant) + staurosporine<br />
**[[5e8y]] – hTGFBR-II kinase domain (mutant) + staurosporine<br />
**[[5e92]] – hTGFBR-II kinase domain (mutant) + AMPPNP<br />
**[[5e92]] – hTGFBR-II kinase domain (mutant) + AMPPNP<br />
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**[[1ks6]] – cTGFBR-II extracellular domain - chicken<br />
+
**[[5qin]], [[5e91]] – hTGFBR-II kinase domain + inhibitor <br />
**[[1ktz]] – hTGFBR-II extracellular domain + TGF-β3 <br />
**[[1ktz]] – hTGFBR-II extracellular domain + TGF-β3 <br />
**[[5ty4]] – hTGFBR-II extracellular domain + mmTGF-β2 <br />
**[[5ty4]] – hTGFBR-II extracellular domain + mmTGF-β2 <br />
**[[5tx4]] – mTGFBR-II extracellular domain (mutant) + hTGF-β2 - mouse<br />
**[[5tx4]] – mTGFBR-II extracellular domain (mutant) + hTGF-β2 - mouse<br />
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**[[1ks6]] – cTGFBR-II extracellular domain - chicken<br />
* TGF-β receptor III
* TGF-β receptor III

Revision as of 11:20, 16 February 2020

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

Drag the structure with the mouse to rotate

3D Structures of TGF-β receptor

Updated on 16-February-2020

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

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Michal Harel, Alexander Berchansky, Jaime Prilusky

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