8ter: Difference between revisions

Latest revision as of 10:05, 20 December 2023

Tropomyosin-receptor kinase fused gene protein (TRK-fused gene protein; TFG) Low Complexity Domain (residues 237-327) P285L mutant, amyloid fiber

Structural highlights

8ter is a 20 chain structure with sequence from Homo sapiens and Purpureocillium lilacinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.59Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

TFG_HUMAN Autosomal recessive spastic paraplegia type 57;Extraskeletal myxoid chondrosarcoma;Autosomal dominant Charcot-Marie-Tooth disease type 2 due to TFG mutation;Hereditary motor and sensory neuropathy, Okinawa type;Differentiated thyroid carcinoma. A chromosomal aberration involving TFG is found in papillary thyroid carcinomas (PTCs). Translocation t(1;3)(q21;q11) with NTRK1. The TFG sequence is fused to the 3'-end of NTRK1 generating the TRKT3 (TRK-T3) fusion transcript.^[1] The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.

Function

TFG_HUMAN Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858).^[2] ^[3] ^[4] A0A2U3DNX3_PURLI

References

↑ Greco A, Mariani C, Miranda C, Lupas A, Pagliardini S, Pomati M, Pierotti MA. The DNA rearrangement that generates the TRK-T3 oncogene involves a novel gene on chromosome 3 whose product has a potential coiled-coil domain. Mol Cell Biol. 1995 Nov;15(11):6118-27. PMID:7565764 doi:10.1128/MCB.15.11.6118
↑ Witte K, Schuh AL, Hegermann J, Sarkeshik A, Mayers JR, Schwarze K, Yates JR 3rd, Eimer S, Audhya A. TFG-1 function in protein secretion and oncogenesis. Nat Cell Biol. 2011 May;13(5):550-8. PMID:21478858 doi:10.1038/ncb2225
↑ Beetz C, Johnson A, Schuh AL, Thakur S, Varga RE, Fothergill T, Hertel N, Bomba-Warczak E, Thiele H, Nürnberg G, Altmüller J, Saxena R, Chapman ER, Dent EW, Nürnberg P, Audhya A. Inhibition of TFG function causes hereditary axon degeneration by impairing endoplasmic reticulum structure. Proc Natl Acad Sci U S A. 2013 Mar 26;110(13):5091-6. PMID:23479643 doi:10.1073/pnas.1217197110
↑ Kanadome T, Shibata H, Kuwata K, Takahara T, Maki M. The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein. FEBS J. 2017 Jan;284(1):56-76. PMID:27813252 doi:10.1111/febs.13949

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OCA

[1] Greco A, Mariani C, Miranda C, Lupas A, Pagliardini S, Pomati M, Pierotti MA. The DNA rearrangement that generates the TRK-T3 oncogene involves a novel gene on chromosome 3 whose product has a potential coiled-coil domain. Mol Cell Biol. 1995 Nov;15(11):6118-27. PMID:7565764 doi:10.1128/MCB.15.11.6118

[2] Witte K, Schuh AL, Hegermann J, Sarkeshik A, Mayers JR, Schwarze K, Yates JR 3rd, Eimer S, Audhya A. TFG-1 function in protein secretion and oncogenesis. Nat Cell Biol. 2011 May;13(5):550-8. PMID:21478858 doi:10.1038/ncb2225

[3] Beetz C, Johnson A, Schuh AL, Thakur S, Varga RE, Fothergill T, Hertel N, Bomba-Warczak E, Thiele H, Nürnberg G, Altmüller J, Saxena R, Chapman ER, Dent EW, Nürnberg P, Audhya A. Inhibition of TFG function causes hereditary axon degeneration by impairing endoplasmic reticulum structure. Proc Natl Acad Sci U S A. 2013 Mar 26;110(13):5091-6. PMID:23479643 doi:10.1073/pnas.1217197110

[4] Kanadome T, Shibata H, Kuwata K, Takahara T, Maki M. The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein. FEBS J. 2017 Jan;284(1):56-76. PMID:27813252 doi:10.1111/febs.13949

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8ter is ON HOLD  until Paper Publication
+==Tropomyosin-receptor kinase fused gene protein (TRK-fused gene protein; TFG) Low Complexity Domain (residues 237-327) P285L mutant, amyloid fiber==
+<StructureSection load='8ter' size='340' side='right'caption='[[8ter]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
-Authors: Rosenberg, G.M., Sawaya, M.R., Boyer, D.R., Ge, P., Abskharon, R., Eisenberg, D.S.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8ter]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Purpureocillium_lilacinum Purpureocillium lilacinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TER FirstGlance]. <br>
-Description: Tropomyosin-receptor kinase fused gene protein (TRK-fused gene protein; TFG) Low Complexity Domain (residues 237-327) P285L mutant, amyloid fiber
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.59&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ter OCA], [https://pdbe.org/8ter PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ter RCSB], [https://www.ebi.ac.uk/pdbsum/8ter PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ter ProSAT]</span></td></tr>
-[[Category: Sawaya, M.R]]
+</table>
-[[Category: Rosenberg, G.M]]
+== Disease ==
-[[Category: Eisenberg, D.S]]
+[https://www.uniprot.org/uniprot/TFG_HUMAN TFG_HUMAN] Autosomal recessive spastic paraplegia type 57;Extraskeletal myxoid chondrosarcoma;Autosomal dominant Charcot-Marie-Tooth disease type 2 due to TFG mutation;Hereditary motor and sensory neuropathy, Okinawa type;Differentiated thyroid carcinoma. A chromosomal aberration involving TFG is found in papillary thyroid carcinomas (PTCs). Translocation t(1;3)(q21;q11) with NTRK1. The TFG sequence is fused to the 3'-end of NTRK1 generating the TRKT3 (TRK-T3) fusion transcript.<ref>PMID:7565764</ref>   The disease is caused by variants affecting the gene represented in this entry.  The disease is caused by variants affecting the gene represented in this entry.
-[[Category: Ge, P]]
+== Function ==
-[[Category: Boyer, D.R]]
+[https://www.uniprot.org/uniprot/TFG_HUMAN TFG_HUMAN] Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858).<ref>PMID:21478858</ref> <ref>PMID:23479643</ref> <ref>PMID:27813252</ref> [https://www.uniprot.org/uniprot/A0A2U3DNX3_PURLI A0A2U3DNX3_PURLI]
-[[Category: Abskharon, R]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Purpureocillium lilacinum]]
+[[Category: Abskharon R]]
+[[Category: Boyer DR]]
+[[Category: Eisenberg DS]]
+[[Category: Ge P]]
+[[Category: Rosenberg GM]]
+[[Category: Sawaya MR]]

8ter: Difference between revisions

Latest revision as of 10:05, 20 December 2023

Tropomyosin-receptor kinase fused gene protein (TRK-fused gene protein; TFG) Low Complexity Domain (residues 237-327) P285L mutant, amyloid fiber

Structural highlights

Disease

Function

References

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