9hvy: Difference between revisions

Latest revision as of 11:03, 10 February 2026

Cryo-EM structure of human separase-SCC1 (1-631) fusion protein

Structural highlights

9hvy is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.5Å
Ligands:	ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

RAD21_HUMAN Cornelia de Lange syndrome. The disease is caused by mutations affecting the gene represented in this entry.^[1]

Function

RAD21_HUMAN Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Also plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway.^[2] ^[3] ESPL1_HUMAN Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms.^[4] ^[5]

References

↑ Deardorff MA, Wilde JJ, Albrecht M, Dickinson E, Tennstedt S, Braunholz D, Monnich M, Yan Y, Xu W, Gil-Rodriguez MC, Clark D, Hakonarson H, Halbach S, Michelis LD, Rampuria A, Rossier E, Spranger S, Van Maldergem L, Lynch SA, Gillessen-Kaesbach G, Ludecke HJ, Ramsay RG, McKay MJ, Krantz ID, Xu H, Horsfield JA, Kaiser FJ. RAD21 mutations cause a human cohesinopathy. Am J Hum Genet. 2012 Jun 8;90(6):1014-27. doi: 10.1016/j.ajhg.2012.04.019. Epub, 2012 May 24. PMID:22633399 doi:https://dx.doi.org/10.1016/j.ajhg.2012.04.019
↑ Pati D, Zhang N, Plon SE. Linking sister chromatid cohesion and apoptosis: role of Rad21. Mol Cell Biol. 2002 Dec;22(23):8267-77. PMID:12417729
↑ Chen F, Kamradt M, Mulcahy M, Byun Y, Xu H, McKay MJ, Cryns VL. Caspase proteolysis of the cohesin component RAD21 promotes apoptosis. J Biol Chem. 2002 May 10;277(19):16775-81. Epub 2002 Mar 1. PMID:11875078 doi:https://dx.doi.org/10.1074/jbc.M201322200
↑ Zou H, McGarry TJ, Bernal T, Kirschner MW. Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis. Science. 1999 Jul 16;285(5426):418-22. PMID:10411507 doi:10.1126/science.285.5426.418
↑ Hauf S, Waizenegger IC, Peters JM. Cohesin cleavage by separase required for anaphase and cytokinesis in human cells. Science. 2001 Aug 17;293(5533):1320-3. PMID:11509732 doi:10.1126/science.1061376

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Deardorff MA, Wilde JJ, Albrecht M, Dickinson E, Tennstedt S, Braunholz D, Monnich M, Yan Y, Xu W, Gil-Rodriguez MC, Clark D, Hakonarson H, Halbach S, Michelis LD, Rampuria A, Rossier E, Spranger S, Van Maldergem L, Lynch SA, Gillessen-Kaesbach G, Ludecke HJ, Ramsay RG, McKay MJ, Krantz ID, Xu H, Horsfield JA, Kaiser FJ. RAD21 mutations cause a human cohesinopathy. Am J Hum Genet. 2012 Jun 8;90(6):1014-27. doi: 10.1016/j.ajhg.2012.04.019. Epub, 2012 May 24. PMID:22633399 doi:https://dx.doi.org/10.1016/j.ajhg.2012.04.019

[2] Pati D, Zhang N, Plon SE. Linking sister chromatid cohesion and apoptosis: role of Rad21. Mol Cell Biol. 2002 Dec;22(23):8267-77. PMID:12417729

[3] Chen F, Kamradt M, Mulcahy M, Byun Y, Xu H, McKay MJ, Cryns VL. Caspase proteolysis of the cohesin component RAD21 promotes apoptosis. J Biol Chem. 2002 May 10;277(19):16775-81. Epub 2002 Mar 1. PMID:11875078 doi:https://dx.doi.org/10.1074/jbc.M201322200

[4] Zou H, McGarry TJ, Bernal T, Kirschner MW. Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis. Science. 1999 Jul 16;285(5426):418-22. PMID:10411507 doi:10.1126/science.285.5426.418

[5] Hauf S, Waizenegger IC, Peters JM. Cohesin cleavage by separase required for anaphase and cytokinesis in human cells. Science. 2001 Aug 17;293(5533):1320-3. PMID:11509732 doi:10.1126/science.1061376

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[3]

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[5]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9hvy is ON HOLD  until Paper Publication
+==Cryo-EM structure of human separase-SCC1 (1-631) fusion protein==
+<StructureSection load='9hvy' size='340' side='right'caption='[[9hvy]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
-Authors: Yu, J., Schmidt, S., Botto, M., Boland, A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9hvy]] is a 1 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=9HVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HVY FirstGlance]. <br>
-Description: Cryo-EM structure of human separase-SCC1 (1-631) fusion protein
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-[[Category: Botto, M]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9hvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hvy OCA], [https://pdbe.org/9hvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hvy RCSB], [https://www.ebi.ac.uk/pdbsum/9hvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hvy ProSAT]</span></td></tr>
-[[Category: Schmidt, S]]
+</table>
-[[Category: Boland, A]]
+== Disease ==
-[[Category: Yu, J]]
+[https://www.uniprot.org/uniprot/RAD21_HUMAN RAD21_HUMAN] Cornelia de Lange syndrome. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:22633399</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/RAD21_HUMAN RAD21_HUMAN] Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Also plays a role in apoptosis, via its cleavage by caspase-3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C-terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway.<ref>PMID:12417729</ref> <ref>PMID:11875078</ref> [https://www.uniprot.org/uniprot/ESPL1_HUMAN ESPL1_HUMAN] Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms.<ref>PMID:10411507</ref> <ref>PMID:11509732</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Boland A]]
+[[Category: Botto M]]
+[[Category: Schmidt S]]
+[[Category: Yu J]]

9hvy: Difference between revisions

Latest revision as of 11:03, 10 February 2026

Cryo-EM structure of human separase-SCC1 (1-631) fusion protein

Structural highlights

Disease

Function

References

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