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==CRYSTAL STRUCTURE OF THE HUMAN CPSF160-WDR33 COMPLEX== | |||
<StructureSection load='6f9n' size='340' side='right' caption='[[6f9n]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f9n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F9N FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f9n OCA], [http://pdbe.org/6f9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f9n RCSB], [http://www.ebi.ac.uk/pdbsum/6f9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f9n ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CPSF1_HUMAN CPSF1_HUMAN]] Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction.<ref>PMID:14749727</ref> [[http://www.uniprot.org/uniprot/WDR33_HUMAN WDR33_HUMAN]] Essential for both cleavage and polyadenylation of pre-mRNA 3' ends.<ref>PMID:19217410</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
3' polyadenylation is a key step in eukaryotic mRNA biogenesis. In mammalian cells, this process is dependent on the recognition of the hexanucleotide AAUAAA motif in the pre-mRNA polyadenylation signal by the Cleavage and Polyadenylation Specificity Factor (CPSF) complex. A core CPSF complex comprising CPSF160, WDR33, CPSF30 and Fip1 is sufficient for AAUAAA motif recognition, yet the molecular interactions underpinning its assembly and mechanism of PAS recognition are not understood. Based on cross-linking-coupled mass spectrometry, crystal structure of the CPSF160-WDR33 subcomplex and biochemical assays, we define the molecular architecture of the core human CPSF complex, identifying specific domains involved in inter-subunit interactions. In addition to zinc finger domains in CPSF30, we identify using quantitative RNA binding assays an N-terminal lysine/arginine-rich motif in WDR33 as a critical determinant of specific AAUAAA motif recognition. Together, these results shed light on the function of CPSF in mediating PAS-dependent RNA cleavage and polyadenylation. | |||
Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex.,Clerici M, Faini M, Aebersold R, Jinek M Elife. 2017 Dec 23;6. doi: 10.7554/eLife.33111. PMID:29274231<ref>PMID:29274231</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6f9n" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clerici, M]] | |||
[[Category: Jinek, M]] | [[Category: Jinek, M]] | ||
[[Category: | [[Category: 3' end processing]] | ||
[[Category: Beta propeller]] | |||
[[Category: Cpsf]] | |||
[[Category: Mrna]] | |||
[[Category: Polyadenylation]] | |||
[[Category: Rna binding protein]] | |||
Latest revision as of 08:53, 3 January 2018
CRYSTAL STRUCTURE OF THE HUMAN CPSF160-WDR33 COMPLEXCRYSTAL STRUCTURE OF THE HUMAN CPSF160-WDR33 COMPLEX
Structural highlights
Function[CPSF1_HUMAN] Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction.[1] [WDR33_HUMAN] Essential for both cleavage and polyadenylation of pre-mRNA 3' ends.[2] Publication Abstract from PubMed3' polyadenylation is a key step in eukaryotic mRNA biogenesis. In mammalian cells, this process is dependent on the recognition of the hexanucleotide AAUAAA motif in the pre-mRNA polyadenylation signal by the Cleavage and Polyadenylation Specificity Factor (CPSF) complex. A core CPSF complex comprising CPSF160, WDR33, CPSF30 and Fip1 is sufficient for AAUAAA motif recognition, yet the molecular interactions underpinning its assembly and mechanism of PAS recognition are not understood. Based on cross-linking-coupled mass spectrometry, crystal structure of the CPSF160-WDR33 subcomplex and biochemical assays, we define the molecular architecture of the core human CPSF complex, identifying specific domains involved in inter-subunit interactions. In addition to zinc finger domains in CPSF30, we identify using quantitative RNA binding assays an N-terminal lysine/arginine-rich motif in WDR33 as a critical determinant of specific AAUAAA motif recognition. Together, these results shed light on the function of CPSF in mediating PAS-dependent RNA cleavage and polyadenylation. Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex.,Clerici M, Faini M, Aebersold R, Jinek M Elife. 2017 Dec 23;6. doi: 10.7554/eLife.33111. PMID:29274231[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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