5w2l: Difference between revisions
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==Structure of a central domain of human Ctc1== | |||
<StructureSection load='5w2l' size='340' side='right' caption='[[5w2l]], [[Resolution|resolution]] 1.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5w2l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W2L FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=5w2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w2l OCA], [http://pdbe.org/5w2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w2l RCSB], [http://www.ebi.ac.uk/pdbsum/5w2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w2l ProSAT]</span></td></tr> | ||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/CTC1_HUMAN CTC1_HUMAN]] Coats plus syndrome;Dyskeratosis congenita. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CTC1_HUMAN CTC1_HUMAN]] Component of the CST complex proposed to act as a specialized replication factor promoting DNA replication under conditions of replication stress or natural replication barriers such as the telomere duplex. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. Initially the CST complex has been proposed to protect telomeres from DNA degradation (PubMed:19854130). However, the CST complex has been shown to be involved in several aspects of telomere replication. The CST complex inhibits telomerase and is involved in telomere length homeostasis; it is proposed to bind to newly telomerase-synthesized 3' overhangs and to terminate telomerase action implicating the association with the ACD:POT1 complex thus interfering with its telomerase stimulation activity. The CST complex is also proposed to be involved in fill-in synthesis of the telomeric C-strand probably implicating recruitment and activation of DNA polymerase alpha (PubMed:22763445). The CST complex facilitates recovery from many forms of exogenous DNA damage; seems to be involved in the re-initiation of DNA replication at repaired forks and/or dormant origins (PubMed:25483097). Involved in telomere maintenance (PubMed:19854131, PubMed:22863775). Involved in genome stability (PubMed:22863775). May be in involved in telomeric C-strand fill-in during late S/G2 phase (By similarity).[UniProtKB:Q5SUQ9]<ref>PMID:19854130</ref> <ref>PMID:19854131</ref> <ref>PMID:22763445</ref> <ref>PMID:22863775</ref> <ref>PMID:25483097</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Rice, C]] | [[Category: Rice, C]] | ||
[[Category: Skordalakes, E]] | [[Category: Skordalakes, E]] | ||
[[Category: Cst complex]] | |||
[[Category: Ctc1]] | |||
[[Category: Dna binding protein]] | |||
[[Category: Telomere]] | |||
