4psi: Difference between revisions

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==PIH1D1/phospho-Tel2 complex==
==PIH1D1/phospho-Tel2 complex==
<StructureSection load='4psi' size='340' side='right' caption='[[4psi]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='4psi' size='340' side='right'caption='[[4psi]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4psi]] is a 4 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=4PSI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PSI FirstGlance]. <br>
<table><tr><td colspan='2'>[[4psi]] is a 4 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=4PSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PSI FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4psf|4psf]]</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=4psi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psi OCA], [https://pdbe.org/4psi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4psi RCSB], [https://www.ebi.ac.uk/pdbsum/4psi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4psi ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIH1D1, NOP17 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4psi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psi OCA], [http://pdbe.org/4psi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4psi RCSB], [http://www.ebi.ac.uk/pdbsum/4psi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4psi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TELO2_HUMAN TELO2_HUMAN]] Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation.<ref>PMID:12670948</ref> <ref>PMID:20810650</ref> 
[https://www.uniprot.org/uniprot/PIHD1_HUMAN PIHD1_HUMAN]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Boulton, S J]]
[[Category: Large Structures]]
[[Category: Flower, T G]]
[[Category: Boulton SJ]]
[[Category: Horejsi, Z]]
[[Category: Flower TG]]
[[Category: Smerdon, S J]]
[[Category: Horejsi Z]]
[[Category: Stach, L]]
[[Category: Smerdon SJ]]
[[Category: Alpha]]
[[Category: Stach L]]
[[Category: Beta]]
[[Category: Phospho-binding]]
[[Category: Phsophorylation]]
[[Category: Protein binding]]
[[Category: Tel2]]

Revision as of 10:28, 8 February 2023

PIH1D1/phospho-Tel2 complexPIH1D1/phospho-Tel2 complex

Structural highlights

4psi is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PIHD1_HUMAN

Publication Abstract from PubMed

The R2TP cochaperone complex plays a critical role in the assembly of multisubunit machines, including small nucleolar ribonucleoproteins (snoRNPs), RNA polymerase II, and the mTORC1 and SMG1 kinase complexes, but the molecular basis of substrate recognition remains unclear. Here, we describe a phosphopeptide binding domain (PIH-N) in the PIH1D1 subunit of the R2TP complex that preferentially binds to highly acidic phosphorylated proteins. A cocrystal structure of a PIH-N domain/TEL2 phosphopeptide complex reveals a highly specific phosphopeptide recognition mechanism in which Lys57 and 64 in PIH1D1, along with a conserved DpSDD phosphopeptide motif within TEL2, are essential and sufficient for binding. Proteomic analysis of PIH1D1 interactors identified R2TP complex substrates that are recruited by the PIH-N domain in a sequence-specific and phosphorylation-dependent manner suggestive of a common mechanism of substrate recognition. We propose that protein complexes assembled by the R2TP complex are defined by phosphorylation of a specific motif and recognition by the PIH1D1 subunit.

Phosphorylation-Dependent PIH1D1 Interactions Define Substrate Specificity of the R2TP Cochaperone Complex.,Horejsi Z, Stach L, Flower TG, Joshi D, Flynn H, Skehel JM, O'Reilly NJ, Ogrodowicz RW, Smerdon SJ, Boulton SJ Cell Rep. 2014 Apr 10;7(1):19-26. doi: 10.1016/j.celrep.2014.03.013. Epub 2014, Mar 20. PMID:24656813[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Horejsi Z, Stach L, Flower TG, Joshi D, Flynn H, Skehel JM, O'Reilly NJ, Ogrodowicz RW, Smerdon SJ, Boulton SJ. Phosphorylation-Dependent PIH1D1 Interactions Define Substrate Specificity of the R2TP Cochaperone Complex. Cell Rep. 2014 Apr 10;7(1):19-26. doi: 10.1016/j.celrep.2014.03.013. Epub 2014, Mar 20. PMID:24656813 doi:http://dx.doi.org/10.1016/j.celrep.2014.03.013

4psi, resolution 2.45Å

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