5g49

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5g49" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5g49 is ON HOLD until Paper Publication
+
==Crystal structure of the Arabodopsis thaliana histone-fold dimer L1L NF-YC3==
 +
<StructureSection load='5g49' size='340' side='right' caption='[[5g49]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5g49]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G49 FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g49 OCA], [http://pdbe.org/5g49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g49 RCSB], [http://www.ebi.ac.uk/pdbsum/5g49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g49 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/NFYB6_ARATH NFYB6_ARATH]] Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters. Plays a role in the regulation of the embryogenesis. Involved in the abscisic acid (ABA) signaling pathway.<ref>PMID:12509518</ref> <ref>PMID:17322342</ref> [[http://www.uniprot.org/uniprot/NFYC3_ARATH NFYC3_ARATH]] Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The structural analysis of the L1L/NF-YC3 histone dimer from A. thaliana shows that it can trimerize and bind to the CCAAT box. Specific sequence and structural features at the protein/DNA interface, in particular the presence of a Asp-His pair, help explain the molecular mechanisms of LEC1/L1L activity as a bona fide mammalian-like NF-YB.
-
Authors: Gnesutta, N., Saad, D., Chaves-Sanjuan, A., Mantovani, R., Nardini, M.
+
Crystal structure of the Arabidopsis thaliana L1L/NF-YC3 histone-fold dimer reveals specificities of the LEC1 family of NF-Y subunits in plants.,Gnesutta N, Saad D, Chaves-Sanjuan A, Mantovani R, Nardini M Mol Plant. 2016 Nov 18. pii: S1674-2052(16)30276-3. doi:, 10.1016/j.molp.2016.11.006. PMID:27871811<ref>PMID:27871811</ref>
-
Description: Crystal structure of the Arabodopsis thaliana histone-fold dimer L1L NF-YC3
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 5g49" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Chaves-Sanjuan, A]]
[[Category: Chaves-Sanjuan, A]]
[[Category: Gnesutta, N]]
[[Category: Gnesutta, N]]
 +
[[Category: Mantovani, R]]
[[Category: Nardini, M]]
[[Category: Nardini, M]]
[[Category: Saad, D]]
[[Category: Saad, D]]
-
[[Category: Mantovani, R]]
+
[[Category: Ccaat box- binding transcription factor]]
 +
[[Category: Histone-fold domain]]
 +
[[Category: Nf-y]]
 +
[[Category: Transcription]]
 +
[[Category: Transcription factor]]

Revision as of 19:36, 9 December 2016

Crystal structure of the Arabodopsis thaliana histone-fold dimer L1L NF-YC3

5g49, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools