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4csr

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Revision as of 07:31, 14 September 2022

High resolution crystal structure of the histone fold dimer (NF-YB)-(NF-YC)

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Retrieved from "http://52.214.119.220/wiki/index.php/4csr"

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 <StructureSection load='4csr' size='340' side='right'caption='[[4csr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4csr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CSR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CSR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4csr]] is a 2 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=4CSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CSR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4csr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4csr OCA], [http://pdbe.org/4csr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4csr RCSB], [http://www.ebi.ac.uk/pdbsum/4csr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4csr 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=4csr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4csr OCA], [https://pdbe.org/4csr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4csr RCSB], [https://www.ebi.ac.uk/pdbsum/4csr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4csr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NFYB_HUMAN NFYB_HUMAN]] Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters, for example in type 1 collagen, albumin and beta-actin genes. [[http://www.uniprot.org/uniprot/NFYC_HUMAN NFYC_HUMAN]] Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters, for example in type 1 collagen, albumin and beta-actin genes.
+[[https://www.uniprot.org/uniprot/NFYB_HUMAN NFYB_HUMAN]] Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters, for example in type 1 collagen, albumin and beta-actin genes.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The sequence-specific transcription factor NF-Y binds the CCAAT box, one of the sequence elements most frequently found in eukaryotic promoters. NF-Y is composed of the NF-YA and NF-YB/NF-YC subunits, the latter two hosting histone-fold domains (HFDs). The crystal structure of NF-Y bound to a 25 bp CCAAT oligonucleotide shows that the HFD dimer binds to the DNA sugar-phosphate backbone, mimicking the nucleosome H2A/H2B-DNA assembly. NF-YA both binds to NF-YB/NF-YC and inserts an alpha helix deeply into the DNA minor groove, providing sequence-specific contacts to the CCAAT box. Structural considerations and mutational data indicate that NF-YB ubiquitination at Lys138 precedes and is equivalent to H2B Lys120 monoubiquitination, important in transcriptional activation. Thus, NF-Y is a sequence-specific transcription factor with nucleosome-like properties of nonspecific DNA binding and helps establish permissive chromatin modifications at CCAAT promoters. Our findings suggest that other HFD-containing proteins may function in similar ways.
-Sequence-Specific Transcription Factor NF-Y Displays Histone-like DNA Binding and H2B-like Ubiquitination.,Nardini M, Gnesutta N, Donati G, Gatta R, Forni C, Fossati A, Vonrhein C, Moras D, Romier C, Bolognesi M, Mantovani R Cell. 2013 Jan 17;152(1-2):132-43. doi: 10.1016/j.cell.2012.11.047. PMID:23332751<ref>PMID:23332751</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4csr" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Nuclear transcription factor Y|Nuclear transcription factor Y]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bolognesi, M]]
+[[Category: Bolognesi M]]
-[[Category: Cocolo, S]]
+[[Category: Cocolo S]]
-[[Category: Gnesutta, N]]
+[[Category: Gnesutta N]]
-[[Category: Mantovani, R]]
+[[Category: Mantovani R]]
-[[Category: Nardini, M]]
+[[Category: Nardini M]]
-[[Category: Ccaat-box]]
-[[Category: Dna-binding]]
-[[Category: Nf-y]]
-[[Category: Transcription]]

4csr

From Proteopedia

Revision as of 07:31, 14 September 2022

High resolution crystal structure of the histone fold dimer (NF-YB)-(NF-YC)

Structural highlights

Function

See Also

Contents

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