1my7: Difference between revisions

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-{{Seed}}
-[[Image:1my7.png|left|200px]]
-<!--
+==NF-kappaB p65 subunit dimerization domain homodimer N202R mutation==
-The line below this paragraph, containing "STRUCTURE_1my7", creates the "Structure Box" on the page.
+<StructureSection load='1my7' size='340' side='right'caption='[[1my7]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1my7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MY7 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#8491;</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=1my7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1my7 OCA], [https://pdbe.org/1my7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1my7 RCSB], [https://www.ebi.ac.uk/pdbsum/1my7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1my7 ProSAT]</span></td></tr>
-{{STRUCTURE_1my7|  PDB=1my7  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TF65_MOUSE TF65_MOUSE] NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression (By similarity). The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1.<ref>PMID:21131967</ref> <ref>PMID:22244329</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/my/1my7_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=1my7 ConSurf].
+<div style="clear:both"></div>
-===NF-kappaB p65 subunit dimerization domain homodimer N202R mutation===
+==See Also==
+*[[NF-kB|NF-kB]]
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_12460563}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 12460563 is the PubMed ID number.
+</StructureSection>
--->
+[[Category: Large Structures]]
-{{ABSTRACT_PUBMED_12460563}}
-==About this Structure==
-MY7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MY7 OCA].
-==Reference==
-Solvent exposed non-contacting amino acids play a critical role in NF-kappaB/IkappaBalpha complex formation., Huxford T, Mishler D, Phelps CB, Huang DB, Sengchanthalangsy LL, Reeves R, Hughes CA, Komives EA, Ghosh G, J Mol Biol. 2002 Dec 6;324(4):587-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12460563 12460563]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Ghosh G]]
-[[Category: Ghosh, G.]]
+[[Category: Huang D-B]]
-[[Category: Huang, D B.]]
+[[Category: Hughes CA]]
-[[Category: Hughes, C A.]]
+[[Category: Huxford T]]
-[[Category: Huxford, T.]]
+[[Category: Komives EA]]
-[[Category: Komives, E A.]]
+[[Category: Mishler D]]
-[[Category: Mishler, D.]]
+[[Category: Phelps CB]]
-[[Category: Phelps, C B.]]
+[[Category: Reeves R]]
-[[Category: Reeves, R.]]
+[[Category: Sengchanthalangsy LL]]
-[[Category: Sengchanthalangsy, L L.]]
-[[Category: Activator]]
-[[Category: Beta-sandwich]]
-[[Category: Beta-sheet]]
-[[Category: Homodimerdna-binding]]
-[[Category: Ig]]
-[[Category: Immunoglobulin]]
-[[Category: Nuclear protein]]
-[[Category: Phosphorylation]]
-[[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:36:06 2008''