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.


6j8y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6j8y is ON HOLD until Jan 21 2021
+
==Crystal structure of the human RAD9-HUS1-RAD1-RHINO complex==
-
 
+
<StructureSection load='6j8y' size='340' side='right'caption='[[6j8y]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[6j8y]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J8Y FirstGlance]. <br>
-
Description:
+
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>
-
[[Category: Unreleased Structures]]
+
<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=6j8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j8y OCA], [http://pdbe.org/6j8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j8y RCSB], [http://www.ebi.ac.uk/pdbsum/6j8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j8y ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/RAD9A_HUMAN RAD9A_HUMAN]] Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.<ref>PMID:10713044</ref> <ref>PMID:21659603</ref> [[http://www.uniprot.org/uniprot/RAD1_HUMAN RAD1_HUMAN]] Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity.<ref>PMID:9660799</ref> <ref>PMID:21659603</ref> [[http://www.uniprot.org/uniprot/HUS1_HUMAN HUS1_HUMAN]] Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase.<ref>PMID:21659603</ref>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Exodeoxyribonuclease III]]
 +
[[Category: Large Structures]]
 +
[[Category: Hara, K]]
 +
[[Category: Hashimoto, H]]
 +
[[Category: Iida, N]]
 +
[[Category: Sakurai, H]]
 +
[[Category: Cell cycle]]
 +
[[Category: Checkpoint]]
 +
[[Category: Dna binding clamp]]
 +
[[Category: Dna damage]]
 +
[[Category: Dna repair]]
 +
[[Category: Exonuclease]]
 +
[[Category: Hydrolase]]
 +
[[Category: Nuclease]]
 +
[[Category: Nucleus]]
 +
[[Category: Pcna]]
 +
[[Category: Phosphoprotein]]

Revision as of 08:01, 4 December 2019

Crystal structure of the human RAD9-HUS1-RAD1-RHINO complex

PDB ID 6j8y

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6j8y"
Personal tools