5yz0

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'''Unreleased structure'''
 
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The entry 5yz0 is ON HOLD
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==Cryo-EM Structure of human ATR-ATRIP complex==
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<SX load='5yz0' size='340' side='right' viewer='molstar' caption='[[5yz0]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yz0]] 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=5YZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YZ0 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.7&#8491;</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=5yz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yz0 OCA], [https://pdbe.org/5yz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yz0 RCSB], [https://www.ebi.ac.uk/pdbsum/5yz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yz0 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ATR_HUMAN ATR_HUMAN] Familial cutaneous telangiectasia and oropharyngeal predisposition cancer syndrome;Seckel syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/ATR_HUMAN ATR_HUMAN] Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at sites of DNA damage, thereby regulating DNA damage response mechanism. Required for FANCD2 ubiquitination. Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication.<ref>PMID:10597277</ref> <ref>PMID:10608806</ref> <ref>PMID:10859164</ref> <ref>PMID:11114888</ref> <ref>PMID:11418864</ref> <ref>PMID:11673449</ref> <ref>PMID:11721054</ref> <ref>PMID:11865061</ref> <ref>PMID:12526805</ref> <ref>PMID:12791985</ref> <ref>PMID:12814551</ref> <ref>PMID:14657349</ref> <ref>PMID:14729973</ref> <ref>PMID:14742437</ref> <ref>PMID:15210935</ref> <ref>PMID:15314022</ref> <ref>PMID:15496423</ref> <ref>PMID:16260606</ref> <ref>PMID:21144835</ref> <ref>PMID:27723717</ref> <ref>PMID:27723720</ref> <ref>PMID:9427750</ref> <ref>PMID:9636169</ref> <ref>PMID:9925639</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ATR (ataxia telangiectasia-mutated and Rad3-related) protein kinase and ATRIP (ATR-interacting protein) form a complex and play a critical role in response to replication stress and DNA damage. Here, we determined the cryo-electron microscopy (EM) structure of the human ATR-ATRIP complex at 4.7 A resolution and built an atomic model of the C-terminal catalytic core of ATR (residues 1 521-2 644) at 3.9 A resolution. The complex adopts a hollow "heart" shape, consisting of two ATR monomers in distinct conformations. The EM map for ATRIP reveals 14 HEAT repeats in an extended "S" shape. The conformational flexibility of ATR allows ATRIP to properly lock the N-termini of the two ATR monomers to favor ATR-ATRIP complex formation and functional diversity. The isolated "head-head" and "tail-tail" each adopts a pseudo 2-fold symmetry. The catalytic pockets face outward and substrate access is not restricted by inhibitory elements. Our studies provide a structural basis for understanding the assembly of the ATR-ATRIP complex and a framework for characterizing ATR-mediated DNA repair pathways.Cell Research advance online publication 22 December 2017; doi:10.1038/cr.2017.158.
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Authors: Qinhui, R., Mengjie, L., Yuan, T., Zihan, W., Hongwei, W., Jiawei, W., Yanhui, X.
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Cryo-EM structure of human ATR-ATRIP complex.,Rao Q, Liu M, Tian Y, Wu Z, Hao Y, Song L, Qin Z, Ding C, Wang HW, Wang J, Xu Y Cell Res. 2017 Dec 22. pii: cr2017158. doi: 10.1038/cr.2017.158. PMID:29271416<ref>PMID:29271416</ref>
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Description: Cryo-EM Structure of human ATR-ATRIP complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Jiawei, W]]
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<div class="pdbe-citations 5yz0" style="background-color:#fffaf0;"></div>
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[[Category: Mengjie, L]]
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[[Category: Yanhui, X]]
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==See Also==
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[[Category: Yuan, T]]
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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[[Category: Qinhui, R]]
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== References ==
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[[Category: Hongwei, W]]
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<references/>
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[[Category: Zihan, W]]
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__TOC__
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</SX>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Liu M]]
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[[Category: Rao Q]]
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[[Category: Tian Y]]
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[[Category: Wang H]]
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[[Category: Wang J]]
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[[Category: Wu Z]]
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[[Category: Xu Y]]

Current revision

Cryo-EM Structure of human ATR-ATRIP complex

5yz0, resolution 4.70Å

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