3hmh

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[[Image:3hmh.png|left|200px]]
 
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==Crystal structure of the second bromodomain of human TBP-associated factor RNA polymerase 1-like (TAF1L)==
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The line below this paragraph, containing "STRUCTURE_3hmh", creates the "Structure Box" on the page.
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<StructureSection load='3hmh' size='340' side='right'caption='[[3hmh]], [[Resolution|resolution]] 2.05&Aring;' 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'>[[3hmh]] 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=3HMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HMH 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">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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=3hmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hmh OCA], [https://pdbe.org/3hmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hmh RCSB], [https://www.ebi.ac.uk/pdbsum/3hmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hmh ProSAT]</span></td></tr>
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{{STRUCTURE_3hmh| PDB=3hmh | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TAF1L_HUMAN TAF1L_HUMAN] May act as a functional substitute for TAF1/TAFII250 during male meiosis, when sex chromosomes are transcriptionally silenced.<ref>PMID:12217962</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/hm/3hmh_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=3hmh 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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Bromodomains (BRDs) are protein interaction modules that specifically recognize epsilon-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. The 61 BRDs in the human genome cluster into eight families based on structure/sequence similarity. Here, we present 29 high-resolution crystal structures, covering all BRD families. Comprehensive crossfamily structural analysis identifies conserved and family-specific structural features that are necessary for specific acetylation-dependent substrate recognition. Screening of more than 30 representative BRDs against systematic histone-peptide arrays identifies new BRD substrates and reveals a strong influence of flanking posttranslational modifications, such as acetylation and phosphorylation, suggesting that BRDs recognize combinations of marks rather than singly acetylated sequences. We further uncovered a structural mechanism for the simultaneous binding and recognition of diverse diacetyl-containing peptides by BRD4. These data provide a foundation for structure-based drug design of specific inhibitors for this emerging target family.
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===Crystal structure of the second bromodomain of human TBP-associated factor RNA polymerase 1-like (TAF1L)===
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Histone recognition and large-scale structural analysis of the human bromodomain family.,Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S Cell. 2012 Mar 30;149(1):214-31. PMID:22464331<ref>PMID:22464331</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_22464331}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3hmh" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 22464331 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22464331}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3hmh]] 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=3HMH OCA].
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==Reference==
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<ref group="xtra">PMID:022464331</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Large Structures]]
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[[Category: Bountra, C.]]
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[[Category: Arrowsmith CH]]
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[[Category: Delft, F von.]]
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[[Category: Bountra C]]
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[[Category: Edwards, A.]]
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[[Category: Edwards A]]
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[[Category: Filippakopoulos, P.]]
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[[Category: Filippakopoulos P]]
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[[Category: Keates, T.]]
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[[Category: Keates T]]
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[[Category: Knapp, S.]]
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[[Category: Knapp S]]
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[[Category: Picaud, S.]]
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[[Category: Picaud S]]
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[[Category: Pike, A C.W.]]
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[[Category: Pike ACW]]
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[[Category: Weigelt, J.]]
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[[Category: Weigelt J]]
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[[Category: Zhang, Y.]]
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[[Category: Zhang Y]]
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[[Category: Bromodomain]]
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[[Category: Von Delft F]]
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[[Category: Cell cycle]]
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[[Category: Disulfide bond]]
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[[Category: Dna-binding]]
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[[Category: Mgc134910]]
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[[Category: Nucleus]]
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[[Category: Sgc]]
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[[Category: Structural genomics consortium]]
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[[Category: Taf2a2]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Current revision

Crystal structure of the second bromodomain of human TBP-associated factor RNA polymerase 1-like (TAF1L)

PDB ID 3hmh

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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