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| | <StructureSection load='6igx' size='340' side='right'caption='[[6igx]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='6igx' size='340' side='right'caption='[[6igx]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6igx]] 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=6IGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6igx]] 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=6IGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IGX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.995Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NCAPG, CAPG, NYMEL3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), NCAPH, BRRN, BRRN1, CAPH, KIAA0074 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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=6igx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6igx OCA], [http://pdbe.org/6igx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6igx RCSB], [http://www.ebi.ac.uk/pdbsum/6igx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6igx ProSAT]</span></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=6igx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6igx OCA], [https://pdbe.org/6igx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6igx RCSB], [https://www.ebi.ac.uk/pdbsum/6igx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6igx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/CND2_HUMAN CND2_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CND3_HUMAN CND3_HUMAN]] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.<ref>PMID:11136719</ref> [[http://www.uniprot.org/uniprot/CND2_HUMAN CND2_HUMAN]] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (PubMed:11136719). Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959).<ref>PMID:11136719</ref> <ref>PMID:27737959</ref> | + | [https://www.uniprot.org/uniprot/CND3_HUMAN CND3_HUMAN] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.<ref>PMID:11136719</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Condensin I is a multi-protein complex that plays an essential role in mitotic chromosome assembly and segregation in eukaryotes. It is composed of five subunits: two SMC (SMC2 and SMC4), a kleisin (CAP-H), and two HEAT-repeat (CAP-D2 and CAP-G) subunits. Although balancing acts of the two HEAT-repeat subunits have been demonstrated to enable this complex to support the dynamic assembly of chromosomal axes in vertebrate cells, its underlying mechanisms remain poorly understood. Here, we report the crystal structure of a human condensin I subcomplex comprising hCAP-G and hCAP-H. hCAP-H binds to the concave surfaces of a harp-shaped HEAT-repeat domain of hCAP-G. Physical interaction between hCAP-G and hCAP-H is indeed essential for mitotic chromosome assembly recapitulated in Xenopus egg cell-free extracts. Furthermore, this study reveals that the human CAP-G-H subcomplex has the ability to interact with not only double-stranded DNA, but also single-stranded DNA, suggesting functional divergence of the vertebrate condensin I complex in proper mitotic chromosome assembly.
| + | |
| | | | |
| - | Structural basis of HEAT-kleisin interactions in the human condensin I subcomplex.,Hara K, Kinoshita K, Migita T, Murakami K, Shimizu K, Takeuchi K, Hirano T, Hashimoto H EMBO Rep. 2019 Mar 11. pii: embr.201847183. doi: 10.15252/embr.201847183. PMID:30858338<ref>PMID:30858338</ref>
| + | ==See Also== |
| - | | + | *[[Condensin|Condensin]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6igx" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hara, K]] | + | [[Category: Hara K]] |
| - | [[Category: Hashimoto, H]] | + | [[Category: Hashimoto H]] |
| - | [[Category: Migita, T]] | + | [[Category: Migita T]] |
| - | [[Category: Shimizu, K]] | + | [[Category: Shimizu K]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Chromosome condensation]]
| + | |
| - | [[Category: Condensin i subunit]]
| + | |
| - | [[Category: Heat repeat]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
