7zeu

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'''Unreleased structure'''
 
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The entry 7zeu is ON HOLD until Paper Publication
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==Crystal structure of human Clusterin, crystal form II==
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<StructureSection load='7zeu' size='340' side='right'caption='[[7zeu]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7zeu]] 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=7ZEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZEU FirstGlance]. <br>
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Description:
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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]] 3.5&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=7zeu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zeu OCA], [https://pdbe.org/7zeu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zeu RCSB], [https://www.ebi.ac.uk/pdbsum/7zeu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zeu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLUS_HUMAN CLUS_HUMAN] Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17407782, PubMed:17412999). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed:2780565). Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).[UniProtKB:P05371][UniProtKB:Q06890]<ref>PMID:11123922</ref> <ref>PMID:12047389</ref> <ref>PMID:12176985</ref> <ref>PMID:12882985</ref> <ref>PMID:16113678</ref> <ref>PMID:17260971</ref> <ref>PMID:17407782</ref> <ref>PMID:17412999</ref> <ref>PMID:17689225</ref> <ref>PMID:19137541</ref> <ref>PMID:19535339</ref> <ref>PMID:19996109</ref> <ref>PMID:20068069</ref> <ref>PMID:21505792</ref> <ref>PMID:22689054</ref> <ref>PMID:24073260</ref> <ref>PMID:2780565</ref> Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity.<ref>PMID:24073260</ref> Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed:21567405).<ref>PMID:21567405</ref> <ref>PMID:24073260</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Bracher A]]
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[[Category: Hartl FU]]
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[[Category: Yuste-Checa P]]

Current revision

Crystal structure of human Clusterin, crystal form II

PDB ID 7zeu

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