1khm

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{{Seed}}
 
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[[Image:1khm.png|left|200px]]
 
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==C-TERMINAL KH DOMAIN OF HNRNP K (KH3)==
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The line below this paragraph, containing "STRUCTURE_1khm", creates the "Structure Box" on the page.
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<StructureSection load='1khm' size='340' side='right'caption='[[1khm]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1khm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KHM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1khm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khm OCA], [https://pdbe.org/1khm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1khm RCSB], [https://www.ebi.ac.uk/pdbsum/1khm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1khm ProSAT]</span></td></tr>
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{{STRUCTURE_1khm| PDB=1khm | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HNRPK_HUMAN HNRPK_HUMAN] One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest.<ref>PMID:16360036</ref> <ref>PMID:20673990</ref> <ref>PMID:22825850</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/1khm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1khm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Among it's many reported functions, heterogeneous nuclear ribonucleoprotein (hnRNP) K is a transcription factor for the c- myc gene, a proto-oncogene critical for the regulation of cell growth and differentiation. We have determined the solution structure of the Gly26--&gt;Arg mutant of the C-terminal K-homology (KH) domain of hnRNP K by NMR spectroscopy. This is the first structure investigation of hnRNP K. Backbone residual dipolar couplings, which provide information that is fundamentally different from the standard NOE-derived distance restraints, were employed to improve structure quality. An independent assessment of structure quality was achieved by comparing the backbone15N T1/T2ratios to the calculated structures. The C-terminal KH module of hnRNP K (KH3) is revealed to be a three-stranded beta-sheet stacked against three alpha-helices, two of which are nearly parallel to the strands of the beta-sheet. The Gly26--&gt;Arg mutation abolishes single-stranded DNA binding without altering the overall fold of the protein. This provides a clue to possible nucleotide binding sites of KH3. It appears unlikely that the solvent-exposed side of the beta-sheet will be the site of protein-nucleic acid complex formation. This is in contrast to the earlier theme for protein-RNA complexes incorporating proteins structurally similar to KH3. We propose that the surface of KH3 that interacts with nucleic acid is comparable to the region of DNA interaction for the double-stranded DNA-binding domain of bovine papillomavirus-1 E2 that has a three-dimensional fold similar to that of KH3.
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===C-TERMINAL KH DOMAIN OF HNRNP K (KH3)===
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High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor.,Baber JL, Libutti D, Levens D, Tjandra N J Mol Biol. 1999 Jun 18;289(4):949-62. PMID:10369774<ref>PMID:10369774</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1khm" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10369774}}, adds the Publication Abstract to the page
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*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10369774 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10369774}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1KHM is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHM OCA].
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==Reference==
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<ref group="xtra">PMID:10369774</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Baber, J.]]
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[[Category: Large Structures]]
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[[Category: Levens, D.]]
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[[Category: Baber J]]
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[[Category: Libutti, D.]]
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[[Category: Levens D]]
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[[Category: Tjandra, N.]]
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[[Category: Libutti D]]
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[[Category: C-myc]]
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[[Category: Tjandra N]]
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[[Category: Dipolar coupling]]
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[[Category: Dna-binding]]
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[[Category: Hnrnp k]]
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[[Category: Kh domain]]
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[[Category: Nmr]]
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[[Category: Rna-binding]]
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[[Category: Three-dimensional structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:47:35 2009''
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Current revision

C-TERMINAL KH DOMAIN OF HNRNP K (KH3)

PDB ID 1khm

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