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1h2i

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Revision as of 09:51, 26 May 2021

Human Rad52 protein, N-terminal domain

Structural highlights

1h2i is a 22 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RAD52_HUMAN] Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.^[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

In eukaryotic cells, RAD52 protein plays a central role in genetic recombination and DNA repair by (i) promoting the annealing of complementary single-stranded DNA and (ii) stimulation of the RAD51 recombinase. The single-strand annealing domain resides in the N-terminal region of the protein and is highly conserved, whereas the nonconserved RAD51-interaction domain is located in the C-terminal region. An N-terminal fragment of human RAD52 (residues 1-209) has been purified to homogeneity and, similar to the full-size protein (residues 1-418), shown to promote single-strand annealing in vitro. We have determined the crystal structure of this single-strand annealing domain at 2.7 A. The structure reveals an undecameric (11) subunit ring with extensive subunit contacts. A large, positively charged groove runs along the surface of the ring, readily suggesting a mechanism by which RAD52 presents the single strand for reannealing with complementary single-stranded DNA.

Structure of the single-strand annealing domain of human RAD52 protein.,Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13492-7. Epub 2002 Oct 7. PMID:12370410^[2]

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

References

↑ Kitao H, Yuan ZM. Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation. J Biol Chem. 2002 Dec 13;277(50):48944-8. Epub 2002 Oct 11. PMID:12379650 doi:10.1074/jbc.M208151200
↑ Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB. Structure of the single-strand annealing domain of human RAD52 protein. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13492-7. Epub 2002 Oct 7. PMID:12370410 doi:10.1073/pnas.212449899

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/1h2i"

@@ Line 3: / Line 3: @@
 <StructureSection load='1h2i' size='340' side='right'caption='[[1h2i]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h2i]] is a 22 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=1H2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H2I FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h2i]] is a 22 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=1H2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2I FirstGlance]. <br>
-</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=1h2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2i OCA], [http://pdbe.org/1h2i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h2i RCSB], [http://www.ebi.ac.uk/pdbsum/1h2i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2i ProSAT]</span></td></tr>
+</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=1h2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2i OCA], [https://pdbe.org/1h2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2i RCSB], [https://www.ebi.ac.uk/pdbsum/1h2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2i ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RAD52_HUMAN RAD52_HUMAN]] Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.<ref>PMID:12379650</ref>
+[[https://www.uniprot.org/uniprot/RAD52_HUMAN RAD52_HUMAN]] Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.<ref>PMID:12379650</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1h2i

From Proteopedia

Revision as of 09:51, 26 May 2021

Human Rad52 protein, N-terminal domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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