1n1j

<table><tr><td colspan='2'>[[1n1j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N1J FirstGlance]. <br>

</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=1n1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1j OCA], [https://pdbe.org/1n1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n1j RCSB], [https://www.ebi.ac.uk/pdbsum/1n1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1j ProSAT]</span></td></tr>

[[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. [[https://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.

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== Publication Abstract from PubMed ==

The heterotrimeric transcription factor NF-Y recognizes with high specificity and affinity the CCAAT regulatory element that is widely represented in promoters and enhancer regions. The CCAAT box acts in concert with neighboring elements, and its bending by NF-Y is thought to be a major mechanism required for transcription activation. We have solved the structure of the NF-YC/NF-YB subcomplex of NF-Y, which shows that the core domains of both proteins interact through histone fold motifs. This histone-like pair is closely related to the H2A/H2B and NC2alpha/NC2beta families, with features that are both common to this class of proteins and unique to NF-Y. The structure together with the modeling of the nonspecific interaction of NF-YC/NF-YB with DNA and the full NF-Y/CCAAT box complex highlight important structural features that account for different and possibly similar biological functions of the transcriptional regulators NF-Y and NC2. In particular, it emphasizes the role of the newly described alphaC helix of NF-YC, which is both important for NF-Y trimerization and a target for regulatory proteins, such as MYC and p53.

The NF-YB/NF-YC structure gives insight into DNA binding and transcription regulation by CCAAT factor NF-Y.,Romier C, Cocchiarella F, Mantovani R, Moras D J Biol Chem. 2003 Jan 10;278(2):1336-45. Epub 2002 Oct 24. PMID:12401788<ref>PMID:12401788</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human]]

[[Category: Cocchiarella, F]]

[[Category: Mantovani, R]]

[[Category: Moras, D]]

[[Category: Romier, C]]

[[Category: Histone-like pair]]