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1h6o

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Revision as of 09:31, 10 January 2018

Dimerisation domain from human TRF1

Structural highlights

1h6o is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1ba5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

TRF1 and TRF2 are key components of vertebrate telomeres. They bind to double-stranded telomeric DNA as homodimers. Dimerization involves the TRF homology (TRFH) domain, which also mediates interactions with other telomeric proteins. The crystal structures of the dimerization domains from human TRF1 and TRF2 were determined at 2.9 and 2.2 A resolution, respectively. Despite a modest sequence identity, the two TRFH domains have the same entirely alpha-helical architecture, resembling a twisted horseshoe. The dimerization interfaces feature unique interactions that prevent heterodimerization. Mutational analysis of TRF1 corroborates the structural data and underscores the importance of the TRFH domain in dimerization, DNA binding, and telomere localization. A possible structural homology between the TRFH domain of fission yeast telomeric protein Taz1 with those of the vertebrate TRFs is suggested.

Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2.,Fairall L, Chapman L, Moss H, de Lange T, Rhodes D Mol Cell. 2001 Aug;8(2):351-61. PMID:11545737^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ de Lange T. Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 2005 Sep 15;19(18):2100-10. PMID:16166375 doi:10.1101/gad.1346005
↑ Fairall L, Chapman L, Moss H, de Lange T, Rhodes D. Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol Cell. 2001 Aug;8(2):351-61. PMID:11545737

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h6o"

@@ Line 1: / Line 1: @@
-==DIMERISATION DOMAIN FROM HUMAN TRF1==
+==Dimerisation domain from human TRF1==
 <StructureSection load='1h6o' size='340' side='right' caption='[[1h6o]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1h6o]] is a 1 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=1H6O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H6O FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ba5|1ba5]]</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=1h6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6o OCA], [http://pdbe.org/1h6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h6o RCSB], [http://www.ebi.ac.uk/pdbsum/1h6o PDBsum]</span></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=1h6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6o OCA], [http://pdbe.org/1h6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h6o RCSB], [http://www.ebi.ac.uk/pdbsum/1h6o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h6o ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/1h6o_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/1h6o_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1h6o

From Proteopedia

Revision as of 09:31, 10 January 2018

Dimerisation domain from human TRF1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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