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<SX load='5vhm' size='340' side='right' viewer='molstar' caption='[[5vhm]], [[Resolution|resolution]] 8.30&Aring;' scene=''>
<SX load='5vhm' size='340' side='right' viewer='molstar' caption='[[5vhm]], [[Resolution|resolution]] 8.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5vhm]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VHM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5VHM FirstGlance]. <br>
<table><tr><td colspan='2'>[[5vhm]] is a 8 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=5VHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VHM FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vgz|5vgz]], [[5vhf|5vhf]], [[5vhh|5vhh]], [[5vhi|5vhi]], [[5vhj|5vhj]], [[5vhn|5vhn]], [[5vho|5vho]], [[5vhp|5vhp]], [[5vhq|5vhq]], [[5vhr|5vhr]], [[5vhs|5vhs]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSMD10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMC2, MSS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMC4, MIP224, TBP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMC6, SUG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMC3, TBP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMC5, SUG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMD2, TRAP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5vhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vhm OCA], [https://pdbe.org/5vhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vhm RCSB], [https://www.ebi.ac.uk/pdbsum/5vhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vhm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5vhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vhm OCA], [http://pdbe.org/5vhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vhm RCSB], [http://www.ebi.ac.uk/pdbsum/5vhm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vhm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PRS6A_HUMAN PRS6A_HUMAN]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). In case of HIV-1 infection, suppresses Tat-mediated transactivation. [[http://www.uniprot.org/uniprot/PRS4_HUMAN PRS4_HUMAN]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. [[http://www.uniprot.org/uniprot/PRS8_HUMAN PRS8_HUMAN]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. [[http://www.uniprot.org/uniprot/PRS7_HUMAN PRS7_HUMAN]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation.<ref>PMID:9295362</ref>  [[http://www.uniprot.org/uniprot/PSMD2_HUMAN PSMD2_HUMAN]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.  Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1. [[http://www.uniprot.org/uniprot/PSD10_HUMAN PSD10_HUMAN]] Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>  Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>  [[http://www.uniprot.org/uniprot/PRS6B_HUMAN PRS6B_HUMAN]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.<ref>PMID:8060531</ref>  [[http://www.uniprot.org/uniprot/PRS10_HUMAN PRS10_HUMAN]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
[https://www.uniprot.org/uniprot/PSD10_HUMAN PSD10_HUMAN] Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>  Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 A resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.
 
Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.,Lu Y, Wu J, Dong Y, Chen S, Sun S, Ma YB, Ouyang Q, Finley D, Kirschner MW, Mao Y Mol Cell. 2017 Jul 20;67(2):322-333.e6. doi: 10.1016/j.molcel.2017.06.007. Epub, 2017 Jul 6. PMID:28689658<ref>PMID:28689658</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vhm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ankyrin 3D structures|Ankyrin 3D structures]]
*[[Proteasome 3D structures|Proteasome 3D structures]]
*[[Proteasome 3D structures|Proteasome 3D structures]]
== References ==
== References ==
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__TOC__
__TOC__
</SX>
</SX>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, S]]
[[Category: Chen S]]
[[Category: Dong, Y]]
[[Category: Dong Y]]
[[Category: Finley, D]]
[[Category: Finley D]]
[[Category: Kirschner, M W]]
[[Category: Kirschner MW]]
[[Category: Lu, Y]]
[[Category: Lu Y]]
[[Category: Ma, Y B]]
[[Category: Ma YB]]
[[Category: Mao, Y]]
[[Category: Mao Y]]
[[Category: Ouyang, Q]]
[[Category: Ouyang Q]]
[[Category: Sun, S]]
[[Category: Sun S]]
[[Category: Wu, J]]
[[Category: Wu J]]
[[Category: 26s proteasome]]
[[Category: Gankyrin]]
[[Category: Hydrolase]]
[[Category: P28]]
[[Category: Regulatory particle]]

Latest revision as of 14:10, 13 March 2024

Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle

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