This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3sjm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:51, 1 March 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 3sjm is ON HOLD until Oct 12 2013
+
==Crystal Structure Analysis of TRF2-Dbd-DNA complex==
-
 
+
<StructureSection load='3sjm' size='340' side='right'caption='[[3sjm]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
-
Authors: Nair, S.K., Sliverman, S.K., Chen, J.H., Xiao, Y.
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[3sjm]] 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=3SJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SJM FirstGlance]. <br>
-
Description: Crystal Structure Analysis of TRF2-Dbd-DNA complex
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</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=3sjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sjm OCA], [https://pdbe.org/3sjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sjm RCSB], [https://www.ebi.ac.uk/pdbsum/3sjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sjm ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TERF2_HUMAN TERF2_HUMAN] Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' 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. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.<ref>PMID:9476899</ref> <ref>PMID:16166375</ref> <ref>PMID:20655466</ref>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Chen JH]]
 +
[[Category: Nair SK]]
 +
[[Category: Sliverman SK]]
 +
[[Category: Xiao Y]]

Current revision

Crystal Structure Analysis of TRF2-Dbd-DNA complex

PDB ID 3sjm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools