3bqo

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Current revision (12:12, 30 August 2023) (edit) (undo)
 
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<StructureSection load='3bqo' size='340' side='right'caption='[[3bqo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3bqo' size='340' side='right'caption='[[3bqo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3bqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BQO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3bqo]] 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=3BQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BQO FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bu8|3bu8]], [[3bua|3bua]]</div></td></tr>
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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]] 2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERF1, PIN2, TRBF1, TRF, TRF1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TINF2, TIN2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3bqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bqo OCA], [https://pdbe.org/3bqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bqo RCSB], [https://www.ebi.ac.uk/pdbsum/3bqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bqo 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=3bqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bqo OCA], [https://pdbe.org/3bqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bqo RCSB], [https://www.ebi.ac.uk/pdbsum/3bqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bqo ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[https://www.uniprot.org/uniprot/TINF2_HUMAN TINF2_HUMAN]] Defects in TINF2 are a cause of dyskeratosis congenita autosomal dominant type 3 (DKCA3) [MIM:[https://omim.org/entry/613990 613990]]. A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.<ref>PMID:18252230</ref> Defects in TINF2 are a cause of retinopathy exudative with bone marrow failure (ERBMF) [MIM:[https://omim.org/entry/268130 268130]]; also known as Revesz syndrome. ERBMF is characterized by bilateral exudative retinopathy, bone marrow hypoplasia, nail dystrophy, fine hair, cerebellar hypoplasia, and growth retardation.<ref>PMID:18252230</ref>
 
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN]] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.<ref>PMID:16166375</ref> [[https://www.uniprot.org/uniprot/TINF2_HUMAN TINF2_HUMAN]] Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly. Isoform 1 may have additional role in tethering telomeres to the nuclear matrix.<ref>PMID:16166375</ref> <ref>PMID:16880378</ref> <ref>PMID:19229133</ref>
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[https://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.<ref>PMID:16166375</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baciu, P]]
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[[Category: Baciu P]]
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[[Category: Chen, Y]]
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[[Category: Chen Y]]
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[[Category: Donigian, J R]]
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[[Category: Donigian JR]]
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[[Category: Lange, T de]]
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[[Category: Lei M]]
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[[Category: Lei, M]]
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[[Category: Yang Y]]
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[[Category: Overbeek, M van]]
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[[Category: De Lange T]]
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[[Category: Yang, Y]]
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[[Category: Van Overbeek M]]
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[[Category: Adp-ribosylation]]
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[[Category: Alternative splicing]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Chromosomal protein]]
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[[Category: Dna binding protein]]
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[[Category: Dna-binding]]
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[[Category: Mitosis]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Telomere]]
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[[Category: Trf1 trfh domain dimerization domain tin2]]
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Current revision

Crystal Structure of TRF1 TRFH domain and TIN2 peptide complex

PDB ID 3bqo

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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