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==NMR Structure of the RNA Binding Domain of Human Fox-1 in Complex with UGCAUGU== | |||
<StructureSection load='2err' size='340' side='right'caption='[[2err]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2err]] is a 2 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=2ERR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERR FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A2BP1, A2BP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2err FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2err OCA], [https://pdbe.org/2err PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2err RCSB], [https://www.ebi.ac.uk/pdbsum/2err PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2err ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/RFOX1_HUMAN RFOX1_HUMAN]] RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis.<ref>PMID:16537540</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/er/2err_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/main_output.php?pdb_ID=2err ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Fox-1 protein regulates alternative splicing of tissue-specific exons by binding to GCAUG elements. Here, we report the solution structure of the Fox-1 RNA binding domain (RBD) in complex with UGCAUGU. The last three nucleotides, UGU, are recognized in a canonical way by the four-stranded beta-sheet of the RBD. In contrast, the first four nucleotides, UGCA, are bound by two loops of the protein in an unprecedented manner. Nucleotides U1, G2, and C3 are wrapped around a single phenylalanine, while G2 and A4 form a base-pair. This novel RNA binding site is independent from the beta-sheet binding interface. Surface plasmon resonance analyses were used to quantify the energetic contributions of electrostatic and hydrogen bond interactions to complex formation and support our structural findings. These results demonstrate the unusual molecular mechanism of sequence-specific RNA recognition by Fox-1, which is exceptional in its high affinity for a defined but short sequence element. | |||
Molecular basis of RNA recognition by the human alternative splicing factor Fox-1.,Auweter SD, Fasan R, Reymond L, Underwood JG, Black DL, Pitsch S, Allain FH EMBO J. 2006 Jan 11;25(1):163-73. Epub 2005 Dec 15. PMID:16362037<ref>PMID:16362037</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2err" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Allain, F H | [[Category: Large Structures]] | ||
[[Category: Auweter, S D | [[Category: Allain, F H]] | ||
[[Category: Auweter, S D]] | |||
[[Category: Protein-rna complex]] | [[Category: Protein-rna complex]] | ||
[[Category: Rna binding protein]] | [[Category: Rna binding protein]] | ||
Latest revision as of 09:55, 9 March 2022
NMR Structure of the RNA Binding Domain of Human Fox-1 in Complex with UGCAUGUNMR Structure of the RNA Binding Domain of Human Fox-1 in Complex with UGCAUGU
Structural highlights
Function[RFOX1_HUMAN] RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis.[1] 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 PubMedThe Fox-1 protein regulates alternative splicing of tissue-specific exons by binding to GCAUG elements. Here, we report the solution structure of the Fox-1 RNA binding domain (RBD) in complex with UGCAUGU. The last three nucleotides, UGU, are recognized in a canonical way by the four-stranded beta-sheet of the RBD. In contrast, the first four nucleotides, UGCA, are bound by two loops of the protein in an unprecedented manner. Nucleotides U1, G2, and C3 are wrapped around a single phenylalanine, while G2 and A4 form a base-pair. This novel RNA binding site is independent from the beta-sheet binding interface. Surface plasmon resonance analyses were used to quantify the energetic contributions of electrostatic and hydrogen bond interactions to complex formation and support our structural findings. These results demonstrate the unusual molecular mechanism of sequence-specific RNA recognition by Fox-1, which is exceptional in its high affinity for a defined but short sequence element. Molecular basis of RNA recognition by the human alternative splicing factor Fox-1.,Auweter SD, Fasan R, Reymond L, Underwood JG, Black DL, Pitsch S, Allain FH EMBO J. 2006 Jan 11;25(1):163-73. Epub 2005 Dec 15. PMID:16362037[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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