2hh2

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{{Seed}}
 
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[[Image:2hh2.png|left|200px]]
 
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==Solution structure of the fourth KH domain of KSRP==
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The line below this paragraph, containing "STRUCTURE_2hh2", creates the "Structure Box" on the page.
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<StructureSection load='2hh2' size='340' side='right'caption='[[2hh2]]' 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'>[[2hh2]] 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=2HH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HH2 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=2hh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hh2 OCA], [https://pdbe.org/2hh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hh2 RCSB], [https://www.ebi.ac.uk/pdbsum/2hh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hh2 ProSAT]</span></td></tr>
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{{STRUCTURE_2hh2| PDB=2hh2 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FUBP2_HUMAN FUBP2_HUMAN] Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs.<ref>PMID:9136930</ref> <ref>PMID:8940189</ref> <ref>PMID:11003644</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/hh/2hh2_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=2hh2 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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The AU-rich element (ARE) RNA-binding protein KSRP (K-homology splicing regulator protein) contains four KH domains and promotes the degradation of specific mRNAs that encode proteins with functions in cellular proliferation and inflammatory response. The fourth KH domain (KH4) is essential for mRNA recognition and decay but requires the third KH domain (KH3) for its function. We show that KH3 and KH4 behave as independent binding modules and can interact with different regions of the AU-rich RNA targets of KSRP. This provides KSRP with the structural flexibility needed to recognize a set of different targets in the context of their 3'UTR structural settings. Surprisingly, we find that KH4 binds to its target AREs with lower affinity than KH3 and that KSRP's mRNA binding, and mRNA degradation activities are closely associated with a conserved structural element of KH4.
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===Solution structure of the fourth KH domain of KSRP===
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The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation.,Garcia-Mayoral MF, Hollingworth D, Masino L, Diaz-Moreno I, Kelly G, Gherzi R, Chou CF, Chen CY, Ramos A Structure. 2007 Apr;15(4):485-98. PMID:17437720<ref>PMID:17437720</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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The line below this paragraph, {{ABSTRACT_PUBMED_17437720}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2hh2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17437720 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17437720}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2HH2 is a [[Single protein]] 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=2HH2 OCA].
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==Reference==
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The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation., Garcia-Mayoral MF, Hollingworth D, Masino L, Diaz-Moreno I, Kelly G, Gherzi R, Chou CF, Chen CY, Ramos A, Structure. 2007 Apr;15(4):485-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17437720 17437720]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Garcia-Mayoral, M F.]]
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[[Category: Garcia-Mayoral MF]]
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[[Category: Kh-rna binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:07:56 2008''
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Current revision

Solution structure of the fourth KH domain of KSRP

PDB ID 2hh2

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