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2ckk

From Proteopedia

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High resolution crystal structure of the human kin17 C-terminal domain containing a kow motif

Structural highlights

2ckk is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.45Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KIN17_HUMAN Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro.[UniProtKB:Q8K339]^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

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

The human KIN17 protein is an essential nuclear protein conserved from yeast to human and expressed ubiquitously in mammals. Suppression of Rts2, the yeast equivalent of gene KIN17, renders the cells unviable, and silencing the human KIN17 gene slows cell growth dramatically. Moreover, the human gene KIN17 is up-regulated following exposure to ionizing radiations and UV light, depending on the integrity of the human global genome repair machinery. Its ectopic over-expression blocks S-phase progression by inhibiting DNA synthesis. The C-terminal region of human KIN17 is crucial for this anti-proliferation effect. Its high-resolution structure, presented here, reveals a tandem of SH3-like subdomains. This domain binds to ribonucleotide homopolymers with the same preferences as the whole protein. Analysis of its structure complexed with tungstate shows structural variability within the domain. The interaction with tungstate is mediated by several lysine residues located within a positively charged groove at the interface between the two subdomains. This groove could be the site of interaction with RNA, since mutagenesis of two of these highly conserved lysine residue weakens RNA binding.

A tandem of SH3-like domains participates in RNA binding in KIN17, a human protein activated in response to genotoxics.,le Maire A, Schiltz M, Stura EA, Pinon-Lataillade G, Couprie J, Moutiez M, Gondry M, Angulo JF, Zinn-Justin S J Mol Biol. 2006 Dec 8;364(4):764-76. Epub 2006 Sep 16. PMID:17045609^[7]

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

References

↑ Biard DS, Miccoli L, Despras E, Frobert Y, Creminon C, Angulo JF. Ionizing radiation triggers chromatin-bound kin17 complex formation in human cells. J Biol Chem. 2002 May 24;277(21):19156-65. PMID:11880372 doi:10.1074/jbc.M200321200
↑ Miccoli L, Biard DS, Créminon C, Angulo JF. Human kin17 protein directly interacts with the simian virus 40 large T antigen and inhibits DNA replication. Cancer Res. 2002 Oct 1;62(19):5425-35 PMID:12359749
↑ Biard DS, Miccoli L, Despras E, Harper F, Pichard E, Créminon C, Angulo JF. Participation of kin17 protein in replication factories and in other DNA transactions mediated by high molecular weight nuclear complexes. Mol Cancer Res. 2003 May;1(7):519-31 PMID:12754299
↑ Miccoli L, Biard DS, Frouin I, Harper F, Maga G, Angulo JF. Selective interactions of human kin17 and RPA proteins with chromatin and the Nucleic Acids Res. 2003 Jul 15;31(14):4162-75. PMID:12853634 doi:10.1093/nar/gkg459
↑ Miccoli L, Frouin I, Novac O, Di Paola D, Harper F, Zannis-Hadjopoulos M, Maga G, Biard DS, Angulo JF. The human stress-activated protein kin17 belongs to the multiprotein DNA replication complex and associates in vivo with mammalian replication origins. Mol Cell Biol. 2005 May;25(9):3814-30. PMID:15831485 doi:10.1128/MCB.25.9.3814-3830.2005
↑ le Maire A, Schiltz M, Stura EA, Pinon-Lataillade G, Couprie J, Moutiez M, Gondry M, Angulo JF, Zinn-Justin S. A tandem of SH3-like domains participates in RNA binding in KIN17, a human protein activated in response to genotoxics. J Mol Biol. 2006 Dec 8;364(4):764-76. Epub 2006 Sep 16. PMID:17045609 doi:10.1016/j.jmb.2006.09.033
↑ le Maire A, Schiltz M, Stura EA, Pinon-Lataillade G, Couprie J, Moutiez M, Gondry M, Angulo JF, Zinn-Justin S. A tandem of SH3-like domains participates in RNA binding in KIN17, a human protein activated in response to genotoxics. J Mol Biol. 2006 Dec 8;364(4):764-76. Epub 2006 Sep 16. PMID:17045609 doi:10.1016/j.jmb.2006.09.033

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/2ckk"

@@ Line 1: / Line 1: @@
-==HIGH RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN KIN17 C-TERMINAL DOMAIN CONTAINING A KOW MOTIF KIN17.==
-<StructureSection load='2ckk' size='340' side='right' caption='[[2ckk]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+==High resolution crystal structure of the human kin17 C-terminal domain containing a kow motif==
+<StructureSection load='2ckk' size='340' side='right'caption='[[2ckk]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ckk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CKK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ckk]] is a 1 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=2CKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</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=2ckk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ckk RCSB], [http://www.ebi.ac.uk/pdbsum/2ckk PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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=2ckk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckk OCA], [https://pdbe.org/2ckk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckk RCSB], [https://www.ebi.ac.uk/pdbsum/2ckk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckk ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/KIN17_HUMAN KIN17_HUMAN] Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro.[UniProtKB:Q8K339]<ref>PMID:11880372</ref> <ref>PMID:12359749</ref> <ref>PMID:12754299</ref> <ref>PMID:12853634</ref> <ref>PMID:15831485</ref> <ref>PMID:17045609</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/2ckk_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/2ckk_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ckk ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 24: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ckk" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 29: / Line 34: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Angulo-Mora, J]]
+[[Category: Large Structures]]
-[[Category: Couprie, J]]
+[[Category: Angulo-Mora J]]
-[[Category: Gondry, M]]
+[[Category: Couprie J]]
-[[Category: Maire, A Le]]
+[[Category: Gondry M]]
-[[Category: Pinon-Lataillade, G]]
+[[Category: Pinon-Lataillade G]]
-[[Category: Schiltz, M]]
+[[Category: Schiltz M]]
-[[Category: Stura, E]]
+[[Category: Stura E]]
-[[Category: Zinn-Justin, S]]
+[[Category: Zinn-Justin S]]
-[[Category: Beta barrel]]
+[[Category: Le Maire A]]
-[[Category: Nuclear protein]]
-[[Category: Ribonucleoprotein]]
-[[Category: Ribosomal protein]]

2ckk

From Proteopedia

Current revision

High resolution crystal structure of the human kin17 C-terminal domain containing a kow motif

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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