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4cse

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==PIH N-terminal domain==
==PIH N-terminal domain==
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<StructureSection load='4cse' size='340' side='right' caption='[[4cse]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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<StructureSection load='4cse' size='340' side='right'caption='[[4cse]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4cse]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CSE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4cse]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CSE FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cgu|4cgu]], [[4cgv|4cgv]], [[4cgw|4cgw]], [[4chh|4chh]], [[4ckt|4ckt]], [[4cv4|4cv4]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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<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=4cse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cse OCA], [http://pdbe.org/4cse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cse RCSB], [http://www.ebi.ac.uk/pdbsum/4cse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cse ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cse OCA], [https://pdbe.org/4cse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cse RCSB], [https://www.ebi.ac.uk/pdbsum/4cse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cse ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TELO2_MOUSE TELO2_MOUSE]] 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 (By similarity).
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[https://www.uniprot.org/uniprot/PIHD1_MOUSE PIHD1_MOUSE]
<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>
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[[Category: Morgan, R M]]
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[[Category: Large Structures]]
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[[Category: Roe, S M]]
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[[Category: Mus musculus]]
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[[Category: Chaperone]]
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[[Category: Morgan RM]]
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[[Category: Molecular chaperone]]
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[[Category: Roe SM]]
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[[Category: Multiprotein complex]]
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[[Category: Phosphorylation]]
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Current revision

PIH N-terminal domain

PDB ID 4cse

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