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==Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF==
==Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF==
<StructureSection load='1nha' size='340' side='right'caption='[[1nha]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1nha' size='340' side='right'caption='[[1nha]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1nha]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NHA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1nha]] 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=1NHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NHA FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAP74 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1nha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nha OCA], [https://pdbe.org/1nha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nha RCSB], [https://www.ebi.ac.uk/pdbsum/1nha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nha ProSAT]</span></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=1nha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nha OCA], [https://pdbe.org/1nha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nha RCSB], [https://www.ebi.ac.uk/pdbsum/1nha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nha ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/T2FA_HUMAN T2FA_HUMAN]] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.<ref>PMID:10428810</ref>
[https://www.uniprot.org/uniprot/T2FA_HUMAN T2FA_HUMAN] TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.<ref>PMID:10428810</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1nha 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=1nha ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
FCP1 (TFIIF-associated CTD phosphatase) is the only known phosphatase specific for the phosphorylated CTD of RNAP II. The phosphatase activity of FCP1 is strongly enhanced by the carboxyl-terminal domain of RAP74 (cterRAP74, residues 436-517), and this stimulatory effect of TFIIF can be blocked by TFIIB. It has been shown that cterRAP74 and the core domain of hTFIIB (TFIIBc, residues 112-316) directly interact with the carboxyl-terminal domain of hFCP1 (cterFCP, residues 879-961), and these interactions may be responsible for the regulatory activities of TFIIF and TFIIB on FCP1. We have determined the NMR solution structure of human cterRAP74, and we have used NMR methods to map the cterFCP-binding sites for both cterRAP74 and human TFIIB. We show that cterFCP binds to a groove of cterRAP74 between alpha-helices H2 and H3, without affecting the secondary structure of cterRAP74. We also show that cterFCP binds to a groove of TFIIBc between alpha-helices D1 and E1 in the first cyclin repeat. We find that the cterFCP-binding site of TFIIBc is very similar to the binding site for the HSV transcriptional activator protein VP16 on the first cyclin repeat of TFIIBc. The cterFCP-binding sites of both RAP74 and TFIIBc form shallow grooves on the protein surface, and they are both rich in hydrophobic and positively charged amino acid residues. These results provide new information about the recognition of acidic-rich activation domains involved in transcriptional regulation, and provide insights into how TFIIF and TFIIB regulate the FCP1 phosphatase activity in vivo.
Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.,Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG Biochemistry. 2003 Feb 18;42(6):1460-9. PMID:12578358<ref>PMID:12578358</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1nha" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, H T]]
[[Category: Chen HT]]
[[Category: Greenblatt, J]]
[[Category: Greenblatt J]]
[[Category: Kobor, M S]]
[[Category: Kobor MS]]
[[Category: Legault, P]]
[[Category: Legault P]]
[[Category: Nguyen, B D]]
[[Category: Nguyen BD]]
[[Category: Omichinski, J G]]
[[Category: Omichinski JG]]
[[Category: Human general transcription factor tfiif]]
[[Category: Rap74]]
[[Category: Transcription]]
[[Category: Transcription factor]]

Revision as of 08:49, 10 April 2024

Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF

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