8i6j: Difference between revisions

Latest revision as of 11:42, 1 February 2024

The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state

Structural highlights

8i6j is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.82Å
Ligands:	ADP
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PDCL3_HUMAN Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (PubMed:23792958, PubMed:26059764). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (PubMed:17429077). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (PubMed:15371430).[UniProtKB:Q4KLJ8]^[1] ^[2] ^[3] ^[4]

References

↑ Wilkinson JC, Richter BW, Wilkinson AS, Burstein E, Rumble JM, Balliu B, Duckett CS. VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that modulates caspase activation. J Biol Chem. 2004 Dec 3;279(49):51091-9. PMID:15371430 doi:10.1074/jbc.M409623200
↑ Stirling PC, Srayko M, Takhar KS, Pozniakovsky A, Hyman AA, Leroux MR. Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression. Mol Biol Cell. 2007 Jun;18(6):2336-45. PMID:17429077 doi:10.1091/mbc.e07-01-0069
↑ Srinivasan S, Meyer RD, Lugo R, Rahimi N. Identification of PDCL3 as a novel chaperone protein involved in the generation of functional VEGF receptor 2. J Biol Chem. 2013 Aug 9;288(32):23171-81. PMID:23792958 doi:10.1074/jbc.M113.473173
↑ Srinivasan S, Chitalia V, Meyer RD, Hartsough E, Mehta M, Harrold I, Anderson N, Feng H, Smith LE, Jiang Y, Costello CE, Rahimi N. Hypoxia-induced expression of phosducin-like 3 regulates expression of VEGFR-2 and promotes angiogenesis. Angiogenesis. 2015 Oct;18(4):449-62. PMID:26059764 doi:10.1007/s10456-015-9468-3

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Wilkinson JC, Richter BW, Wilkinson AS, Burstein E, Rumble JM, Balliu B, Duckett CS. VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that modulates caspase activation. J Biol Chem. 2004 Dec 3;279(49):51091-9. PMID:15371430 doi:10.1074/jbc.M409623200

[2] Stirling PC, Srayko M, Takhar KS, Pozniakovsky A, Hyman AA, Leroux MR. Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression. Mol Biol Cell. 2007 Jun;18(6):2336-45. PMID:17429077 doi:10.1091/mbc.e07-01-0069

[3] Srinivasan S, Meyer RD, Lugo R, Rahimi N. Identification of PDCL3 as a novel chaperone protein involved in the generation of functional VEGF receptor 2. J Biol Chem. 2013 Aug 9;288(32):23171-81. PMID:23792958 doi:10.1074/jbc.M113.473173

[4] Srinivasan S, Chitalia V, Meyer RD, Hartsough E, Mehta M, Harrold I, Anderson N, Feng H, Smith LE, Jiang Y, Costello CE, Rahimi N. Hypoxia-induced expression of phosducin-like 3 regulates expression of VEGFR-2 and promotes angiogenesis. Angiogenesis. 2015 Oct;18(4):449-62. PMID:26059764 doi:10.1007/s10456-015-9468-3

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[3]

[4]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8i6j is ON HOLD  until Paper Publication
+==The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state==
+<StructureSection load='8i6j' size='340' side='right'caption='[[8i6j]], [[Resolution|resolution]] 3.82&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8i6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I6J FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.82&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8i6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i6j OCA], [https://pdbe.org/8i6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i6j RCSB], [https://www.ebi.ac.uk/pdbsum/8i6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i6j ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PDCL3_HUMAN PDCL3_HUMAN] Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (PubMed:23792958, PubMed:26059764). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (PubMed:17429077). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes (By similarity). Modulates the activation of caspases during apoptosis (PubMed:15371430).[UniProtKB:Q4KLJ8]<ref>PMID:15371430</ref> <ref>PMID:17429077</ref> <ref>PMID:23792958</ref> <ref>PMID:26059764</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Kim H]]
+[[Category: Lim S]]
+[[Category: Park J]]
+[[Category: Roh SH]]

8i6j: Difference between revisions

Latest revision as of 11:42, 1 February 2024

The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state

Structural highlights

Function

References

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